Pasta-Filata Cheeses

Chapter 40
Pasta-Filata Cheeses
Donald J. McMahon*, Craig J. Oberg**
*Utah State University, Logan, UT, United States
**Weber State University, Ogden, UT, United States
INTRODUCTION baking on pizza, in which it is specifically manufactured

to melt, flow, and brown, when heated under conditions
This chapter builds upon the chapter on pasta-filata cheese specified by each customer. Another growth area related to
in the previous edition written by Kindstedt et al. (2004). consumption of LMMC is “string” cheese (Mayer, 2011),
Pasta-filata cheeses originated primarily in the greater which is popular in the United States as a snack amongst
northern Mediterranean regions of Italy, Greece, the Bal- children, and increasingly so with adults (including in coun-
kans, Turkey, and Eastern Europe. Today these cheeses are tries where cheeses have not been a part of the traditional
still made in some regions using traditional methods from cuisine). String cheese is a part-skim LMMC that is hot ex-
the milk of cows, goats, sheep, or water buffalo, however, truded ∼1.5 cm diameter, cut into 15-cm lengths, and sold
there is large-scale manufacture of cheeses, such as Mozza- as a snack cheese that is consumed cold.
rella in many countries utilizing new technologies. The pas-
ta-filata cheeses include soft or semisoft cheeses consumed
fresh (e.g., fresh Mozzarella made from whole milk and hav- OVERVIEW OF MANUFACTURING
ing moisture content ∼55% or higher) or after a short aging
TECHNOLOGY
period (e.g., low-moisture part-skim Mozzarella) whereas,
other varieties are hard or semihard ripened cheeses aged for The initial manufacturing process for making LMMC is
longer before consumption (e.g., Caciocavallo, Kashkaval, similar to other rennet-set cheeses, with large scale cheese
Provolone, and Ragusano). The term pasta-filata, which is vats containing up to 40,000 L of milk. When milk is ren-
derived from an Italian phrase that literally means “spun neted, casein micelles are converted from a stable colloid
paste” or “stretched curd”, refers to a unique plasticization into a protein gel with individual casein micelles joined to-
and stretching process shared by all pasta-filata cheeses gether into cross-linked chains (McMahon et al., 1999). As
that provides this diverse group with a common identity. cheesemaking proceeds, whey is expelled from the curd and
This chapter primarily focuses on low-moisture Mozzarella the protein chains become thicker through continued asso-
cheese (LMMC), made from either whole or part-skimmed ciation with one another until they form a three-dimensional
milk, to be used as a pizza cheese, which makes it the most (3D) protein matrix in which water, fat, and starter bacte-
economically important of the pasta-filata cheeses. World- ria are distributed (Oberg et al., 1993; Schmidt, 1982). For
wide production of LMMC far exceeds that of other pasta- LMMC, this process is the same as Cheddar cheese up to
filata cheeses. In countries where American-style pizza is when cheese curds are transferred to a cooker-stretcher to
becoming popular, LMMC is often referred to by consum- undergo the pasta-filata plasticization process. Although it
ers as Mozzarella cheese without any designation of being is possible to manufacture cheese with the same composi-
low-moisture or part-skim Mozzarella cheese. tion as LMMC and similar functional properties without
Annual global production of LMMC continues to grow, the plasticization step, such cheese does not have the same
with 1.6 billion kilograms of Mozzarella cheese produced microstructural appearance. Depending on legal require-
in the United States (USDA, 2014) alone, much of which ments, such cheese may be sold as pizza cheese or even
is manufactured in cheese plants producing up to 1 million as Mozzarella cheese depending on alternative make proce-
kilogram per day. Cheesemaking on this scale requires pre- dure allowances in various countries (Govindasamy-Lucey
cise control over all aspects of the manufacturing process. et al., 2005).
This has fostered development of new manufacturing tech- Much LMMC is manufactured with part-skim milk,
nologies to produce cheeses with well-defined functional although cheeses with higher fat contents are also manufac-
properties suitable for a variety of applications, including tured depending upon desired usage and customer needs.
Cheese: Chemistry, Physics and Microbiology. http://dx.doi.org/10.1016/B978-0-12-417012-4.00040-5
Copyright © 2017 Elsevier Ltd. All rights reserved. 1041
1042 S ECTION | II Diversity of Cheese
To manufacture cheese with 30%–45% fat-in-dry-matter

(FDM) requires standardization of milk to a higher casein-
to-fat ratio than naturally occurs in milk. Standardiza-
tion can be achieved through increasing casein content by
adding skim milk powder, condensed skim milk, or ultra-
filtered milk protein concentrate, with such an increase in
casein content providing increased yield of cheese per vat.
Up to 30% of fat can be lost during LMMC manufacture
(Francolino et al., 2010; Ghiglietti et al., 2005; Rehman
et al., 2003) coming from losses into whey during curd
manufacture and losses as “cooker cream” into the hot water
during plasticization. Extent of fat loss depends upon milk
composition and increasing renneting temperature from 34
to 39°C, which decreases fat recovery (Hussain et al., 2012).
Increasing protein content of milk using ultrafiltration or
adding milk protein concentrate increases yield by increas-
ing both fat and protein recovery (Rehman et al., 2003).
Removal of cream can also be used to standardize the
milk but this results in decreased yields per vat of milk un-
less the standardized milk is subsequently ultrafiltered to
increase protein and fat content. For the pizza industry,
higher moisture content is preferred with fat content ad-
justed depending upon cheese performance requirements
during baking. Higher fat content (45% FDM or higher)
has advantages during high temperature baking conditions
because of such cheese’s increased ease of melting and re-
lease of fat when heated, which is preferred by some quick
service pizza restaurants.
Thermophilic lactic acid bacteria (LAB) (such as Strep-
tococcus thermophilus, Lactobacillus delbrueckii subsp.
bulgaricus, and Lactobacillus helveticus) are used most
throughout the world as starter cultures for making LMMC.
Mesophilic LAB (such as Lactococcus lactis) can also be
used although differences in cheese flavor profile would be
expected. The principal role of starter culture is to suffi-
ciently acidify the milk and subsequent curd via conversion
of lactose into lactic acid so the chemistry of the cheese al-
lows it to be plasticized and stretch when heated in hot wa-
ter. This primarily results from a reduction in the amount of
calcium that remains bound to the caseins in the curd at the
time of stretching (McMahon et al., 2005). Rapid acid pro-
duction by the starter culture decreases the manufacturing FIGURE 40.1 Schematic diagram of formation of network structure
time of LMMC and helps achieve a high moisture content formed by renneting of milk and changes in microstructure that occur
(up to 52%), so in large cheese factories, short manufac- during manufacture of curd and plasticization.
turing times are economically important. Time from ren-
neting to the commencement of stretching has been fur- cheeses with moisture contents of 55%–60% (w/w) that are
ther reduced from ≤180 min (McCoy, 1997) to ≤150 min primarily consumed fresh (Francolino et al., 2010).
(private communication, Dr. Randall Thunell, Providence, Rennet is added to coagulate the milk as occurs in other
UT, USA, 2003). Chemical acidification of milk prior to, rennet-set cheeses (Fig. 40.1). After the casein micelles
or in conjunction with, starter cultures may also be used have aggregated to form a 3D network, the resulting co-
to shorten the manufacturing time or reduce calcium con- agulum is cut into curd pieces to initiate whey syneresis.
tent of the cheese. Complete acidification using acetic acid Since thermophilic cultures are used for LMMC, the milk
or citric acid is not generally used for making LMMC, in is set at about 33–35°C, with the resulting curds and whey
the same way it is utilized for manufacturing Mozzarella stirred and heated to about 40–43°C. Pasta-filata cheeses
Pasta-Filata Cheeses Chapter | 40 1043
FIGURE 40.2 Matted cheese curd placed on a wooden board while fermentation continues, Metsovo, Greece.
designed for aging require a lower moisture content and and whey syneresis. In large operations, this takes place on
may be cooked to about 50°C, whereas high-moisture fresh a draining, matting, and cheddaring belt system. When curd
Mozzarella cheese receives little, if any, cooking. After suf- has reached an optimum calcium content (usually when the
ficient stirring and acid development, whey is partially or curd pH is between 5.2 and 5.3), it is cut or milled into
completely drained (at about pH 6.0–6.2) and the curd is pieces (Figs. 40.3–40.5) in preparation for cooking and
matted (Fig. 40.2) or stirred to allow for further acidification stretching. The milled curd may be partially dry-salted at
FIGURE 40.3 Cutting of Ragusano curd after overnight fermentation into pieces prior to stretching in the CoRFiLaC cheese laboratory,
Ragusa, Siciliy, Italy.
FIGURE 40.4 Cutting of Mozzarella cheese curd after fermentation, Metsovo, Greece.
this stage to incorporate a portion of the salt needed in the structure of the cheese becomes fibrous as the protein por-
final cheese. tion of the curd aligns into fibers with fat globules collected
The curd pieces are then immersed into hot water or into channels between the protein strands (Fig. 40.1), which
brine and mixed to plasticize and stretch the curd. On an allows long strings of cheese to be pulled from the hot
industrial scale, mechanical working of curd occurs in a cheese (Fig. 40.9). If the curd is stretched before sufficient
cooker/stretching apparatus (Fig. 40.6) whereas it was tradi- calcium has been released from the proteins (such as if the
tionally performed by hand using wooden tools (Figs. 40.7 pH is too high), then the cheese becomes too rubbery. If
and 40.8). During the pasta-filata process, the internal acidification of the curd is allowed to continue for a long
FIGURE 40.6 Low-moisture Mozzarella cheese curd being fed into

the hot water hopper of a single screw cooker/stretcher.
FIGURE 40.5 Milling of low-moisture Mozzarella cheese (LMMC)

after fermentation in an enclosed draining, matting and cheddaring
system in a large scale cheese facility.
time, so the curd pH drops below 5.2 and too much cal-
cium is solubilized, then the cheese will become runny and
“soupy” when cooked and stretched.
When the stretching process takes place in a single- or
twin-screw cooker, the inlet hopper of the cooker is filled
with hot water (65–70°C), so that as curd is added and
heated, it undergoes mixing and stretching while being
pushed down the barrel of the cooker/stretcher by the rotat-
ing screw(s). Cheese exits the cooker/stretcher at 55–65°C
as a smooth plastic mass (Fig. 40.10) and is then forced
under pressure into chilled moulds (Fig. 40.11), which
gives the cheese its shape. This sufficiently precools the
block to retain its shape when removed from the mould and
immersed in cold brine (Fig. 40.12). Alternatively, the hot
plastic cheese mass may be extruded as a continuous ribbon
directly into cold water or brine (Barz et al., 1999). When
cooled by brining, the blocks of LMMC should be held in
the brine for sufficient time to cool the internal temperature
to 6°C or less. Insufficient cooling of LMMC blocks be-
fore being vacuum packaged and boxed (or stacked without
packaging) means the interior blocks on a pallet of cheese
will still be warm so excessive breakdown of the proteins
can occur, as well as continued acid development if the salt
FIGURE 40.7 Traditional hand stretching of Ragusano cheese after content is also low (1% or less). There are variations to this
mixing curd with hot water in a copper vessel in the CoRFiLaC cheese basic process of making LMMC but the underlying prin-
laboratory, Ragusa, Sicily, Italy. ciples are the same. As an alternative to shredding or cubing
FIGURE 40.8 Stretching of Provolone cheese with aid of a wooden paddle, Metsovo, Greece.
FIGURE 40.9 Stretch of Oaxaca cheese being demonstrated by Prof. Nana Farkye during a workshop on Hispanic cheeses at the Western Dairy
Center, Logan, Utah, USA.
of LMMC after cooling and brining, Ferrari et al. (2003)

proposed extruding the hot plasticized cheese in consum-
er-usable 2-g pieces (5 × 8 × 40 mm). This increases the
surface-to-volume ratio and decreases cooling time 10-fold,
allowing a decrease in cooling brine volume and brine tank
dimensions.
Only a brief ripening period (usually less than 1 month
at 4°C) is required for LMMC to develop the desired func-
tional properties for use as a pizza ingredient. Typically
after manufacturing, the cheese is not suitable for shred-
ding. After 2 or 3 weeks of refrigerated storage, LMMC
shreds well and develops the desired baking characteris-
tics of good melting with some elasticity of the melted
cheese so it stretches when pulled apart. The cheese loses
its optimum baking properties and melts excessively with
extended storage, that allows continued breakdown of the
proteins.
STEPS IN CHEESE MANUFACTURE

The unique functional properties of Mozzarella cheese
come from distinct, but interdependent phases (Dave et al.,
2003b). The first phase consists of manufacturing curd by
gelation of milk with sufficient expulsion of water as whey
to achieve the cheese moisture target, development of the
appropriate acidity to achieve the target pH, and solubili-
zation of sufficient calcium to obtain the needed balance
between melting/flow and strength of protein–protein in-
teractions so that the cheese stretches when heated. The
second phase involves plasticization of the heated curd and
FIGURE 40.10 Hot plasticized LMMC as it exits the cooker/stretch- an internal reorganization of the cheese microstructure into
er and before molding. fibrous strands during passage through the cooker/stretcher.
FIGURE 40.11 Molding machine for making blocks of LMMC.
The final phase entails cooling of the hot mass of cheese, called casein micelles) (McMahon and Oommen, 2008).
usually with concomitant salt uptake that sets the stage for Casein micelles lose colloidal stability upon cleavage of k-
development of the varied functional properties of melted casein into para-k-casein (which remains part of the casein
LMMC responsible for consumer perceptions (Rowney supramolecule) and a macropeptide portion (also known as
et al., 1999). caseinomacropeptide or glycomacropeptide), which is lost
into the surrounding aqueous environment (McMahon and
Brown, 1984). At cheesemaking temperatures (30–35°C),
Curd Formation and Acid Development
casein supramolecules aggregate, converting milk from a
The caseins in milk are packaged into a stable suspension dispersed colloidal suspension of casein supramolecules
of casein–calcium phosphate supramolecules (commonly into a semisolid gel or curd (Fig. 40.1). This coarse-stranded
FIGURE 40.12 Blocks of LMMC after pre-cooling in the molder and immersed in a brine to complete cooling and final absorption of salt.
FIGURE 40.13 Formation of curd inside a 35,000-L capacity enclosed cheese vat.
gel network entraps fat globules and bacterial cells, and fills
the entire volume of the cheese vat (Fig. 40.13) (Oberg
et al., 1993). This initial gel network is comprised of clus-
ters and chains of individual micelles that have surface con-
tact with each other (Fig. 40.14).
Subsequent changes to the curd during cheesemaking
can be attributed to a shifting balance between entropy-
induced hydrophobic protein–protein interactions and elec-
trostatic/hydrophilic interactions between the caseins and
water brought about by release of the macropeptide portion
of k-casein upon renneting. In essence, the para-caseins
become “sticky” and start to rearrange as the hydrophobic
groups cluster together to shield them from water, and salt
bridges form through interactions with calcium and phos-
phate. As the pH drops, charges on the proteins change. For
example, imidazole side chains of histidine change from
being 60% uncharged at milk pH 6.7, to 60% carrying a
positive charge at cheese pH 5.3. The phosphate groups on
phosphoserine side chains also become more protonated
reducing the negative charge and ability to bind calcium.
Consequently, the lowest free energy state of the curd pro-
tein matrix continually changes, so protein rearrangements
occur during cooking and stirring of the curd. The process
of casein supramolecule destabilization continues (since the FIGURE 40.14 Scanning electron micrograph casein micelle net-
impact of entropic forces increases with temperature) to the work formed after renneting of milk.
FIGURE 40.15 Scanning electron micrograph of low-moisture part-skim Mozzarella cheese after dry stirring, small arrow, curd surface layer, large
arrow, void spaces that contained fat removed during sample preparation. (Reprinted from Oberg, C.J., McManus, W.R., McMahon, D.J., 1993. Micro-
structure of Mozzarella cheese during manufacture. Food Struct. 12, 251–258).
extent that the supramolecules fuse together with a loss of water) can easily diffuse between cells, but as cells begin
the serum originally occluded (Fig. 40.1). It is important to to close (Fig. 40.15) then moisture movement is retarded.
realize that while the casein supramolecules lose their col-
loidal identity, the individual protein molecules retain their Decrease in pH and Calcium Removal
identity, even as they aggregate.
Instead of having chains and clusters of individual casein Reduction in curd pH promotes a number of physico-
supramolecules, thicker, and thicker strands of protein co- chemical conditions, which are conducive to promoting the
alesce as the original chains of casein micelles collapse upon flow of the curd during plasticization (Guinee et al., 2002),
each other. The 3D protein network that supplies the basic including solubilization of colloidal calcium phosphate (van
structure of the curd shrinks with the entrapped whey being Hooydonk et al., 1986), an increase in the ratio of soluble
expelled (McMahon et al., 1993; Oberg et al., 1993). The to colloidal calcium (Guinee et al., 2000), and an increase
fat globules become distorted in shape as they are pushed in para-casein hydration (Creamer, 1985). As described
together by the shrinking protein curd network while the by Pastorino et al. (2003a), the extent of calcium bound to
curd is still warm. This continual mechanical pressure at the protein in cheese curd affects the amount of protein aggre-
microstructure level being exerted by the collapsing protein gation, with higher calcium levels resulting in more exten-
network on the fat globules results in some breakage of the sive protein aggregation, hence larger protein aggregates
fat globule membrane. resulting in a coarser gel network. If calcium is injected
By the time dry-stirring of the curd has been complet- into cheese, increased protein–protein interactions cause a
ed, the curd structure can be represented as an open-celled dehydration of caseins resulting in the protein matrix hav-
gel consisting of a 3D network of protein strands that are ing a decreased capacity to hold water so more syneresis
2–6 µm thick, corresponding to having 15–50 individual occurs. As calcium binds to phosphoserine and carboxylate
casein supramolecules fused together (Fig. 40.15). Between side groups on the caseins, negative charges are neutralized,
the protein strands are open cells that contain fat globules, therefore electrostatic repulsion between proteins decreases
or groups of fat globules, along with bacteria and whey fill- and protein-to-protein interactions, involving hydrophobic
ing up the interstitial spaces. Because of the initial open cell regions, are promoted (Gaucheron et al., 1997). Having a
structure of the cheese matrix, whey constituents (including high level of calcium in the final cheese means the protein
matrix is less hydrated, so more energy must be applied to then drawn by a rotating screw into the barrel of the cooker.
overcome protein–protein interactions to allow protein mol- When the temperature of the curd reaches about 50–55°C, it
ecules to deform when a force is applied (i.e., the cheese becomes plasticized, and is stretched as it moves along the
is harder) or to flow when heated (i.e., the cheese melts barrel. In a single-screw cooker some of the worked cheese
poorly). Therefore, an important aspect of the manufacture mass recirculates back along the space between the barrel
of Mozzarella cheese is to reduce protein-bound calcium wall and the screw flights, and mixes with incoming curd.
through an acidification process. In a twin-screw extruder with counter-rotating screws,
The most effective way to solubilize calcium is to acidify the cooker can be modeled as series of transitional and mix-
the milk before rennet is added (Joshi et al., 2004d) with the ing zones representing flow of molten cheese through the
resulting cheese being softer with a higher moisture (Ong cooker barrel (Yu and Gunasekaran, 2005b). The mixing
et al., 2012) and a different microstructure (Morales-Cela- zones occur between the screws, whereas the transitional
ya et al., 2012). Such preacidification has been the crucial zones occur between each screw and the inner surface of the
cheesemaking modification to increase meltability of lower barrel. In a deep barrel extruder (such as used for Mozza-
fat Mozzarella cheeses (Dave et al., 2003a; McMahon and rella cooking and stretching) there is a velocity distribution
Oberg, 2000; McMahon et al., 2005; Merrill et al., 1994; of the moving cheese. Flow of cheese from the channels of
Paulson et al., 1998; Sheehan and Guinee, 2004; Zisu and each screw collide at the middle, preventing extensive mix-
Shah, 2007). The ability of curd at any fat level to plasticize ing (Yu and Gunasekaran, 2005b) so that downstream flow
in hot water and reorganize into a unidirectional fibrous is dominant.
structure is related to the partial removal of casein-associ- There is also a temperature variation within the barrel
ated calcium phosphate during curd manufacture prior to in which heat is conducted from the barrel and the screw
entering the cooker/stretcher (Guinee et al., 2002; Joshi root into the cheese, and viscous dissipation occurs near the
et al., 2004d; McMahon et al., 2005) with more calcium screw flights where the shear applied to the cheese mass
needing to be removed as the cheese fat content is lowered. is highest. Operating conditions, such as screw speed and
barrel temperature, are not sufficient parameters to describe
the stretching process, so Yu and Gunasekaran (2005b) pro-
Curd Plasticization and Stretching
posed that specific mechanical energy (SME), mean resi-
Prior to heat treatment, the cheese curd consists of an dence time (MRT), and exit temperature be used as control
amorphous 3D protein matrix containing random pockets variables in design and in understanding extruder opera-
of serum and fat globules (Figs. 40.1 and 40.15) (Joshi tional parameters on final cheese functionality.
et al., 2004d; Oberg et al., 1993). In large scale manufacture When screw speed is increased, SME increases as more
of LMMC, stretching is a two-stage process with milled mechanical energy is applied to the cheese, but MRT de-
curd being fed into a reservoir of hot water (typically 65– creases with increase in screw speed. So with a deep barrel
80°C) (Renda et al., 1997) (Fig. 40.16) where it is warmed extruder, the ratio of thermal energy input to mechanical en-
as it settles to the bottom of the mixer. The warmed curd is ergy input is relatively high, so the decreased MRT results
in a lower cheese exit temperature. In contrast, Renda et al.
(1997) observed a lower exit temperature with lower screw
speed while keeping the cooker water temperature con-
stant (57°C). Such different responses of exit temperature
to changes in MRT probably result from the difference in
the design of the cooker that can alter the extent of heating
from the hot cooker water, from the barrel and screw, and
extent of SME input to the cheese mass. When heated (e.g.,
to 55–60°C), the type of fracture of the melted Mozzarella
cheese is of the stick-slip type and requires a critical shear
rate (Bähler and Hinrichs, 2013).
Temperature of the cheese mass and cheese composi-
tion (such as calcium content which affects cheese melting
and stretching) can also affect proper heating of the curd. A
high screw speed and a low water temperature can result in
tearing of the cheese curd that had been warmed sufficiently
to soften and permit deformation and stretching under the
shear force of the screws (Renda et al., 1997). Curd tearing
FIGURE 40.16 Low-moisture Mozzarella cheese that has begun the causes greater moisture and fat losses resulting in LMMC
plasticization process in a single-screw cooker/stretcher. with lower moisture, lower FDM, and a firmer texture. A
decrease in cheese moisture content as SME increased was water or increased MSE during the plasticization process
reported by Yu and Gunasekaran (2005a) who showed a would favor increased hydrophobically-mediated aggrega-
quadratic relationship between exit temperature and mois- tion of the para-casein and a shift toward more insoluble
ture content, between SME and FDM, and between exit protein-bound calcium. This would then produce a more
temperature and FDM. This allows determination of opti- calcium cross-linked, elastic, fibrous structure, and a great-
mum SME and exit temperature values for minimizing fat er phase separation of protein and water. This would extend
loss, and maximizing cheese yield. the time before optimum melting properties are achieved
When the curd is properly plasticized, a higher screw but provide a longer shelf-life in which the LMMC could
speed will reduce MRT, so there is less time for conduc- be shredded satisfactorily, and would slow the softening of
tion of heat into the cheese. If the cooker/stretcher design LMMC when made into string cheese.
imparts high shear, there will be an increase in SME, such In heated and stretched LMMC, the protein matrix
that the temperature increase caused by viscous dissipation becomes molten and starts to fuse together, most likely
more than compensates for less heat transfer by conduction through hydrophobic interactions. Protein strand fusion
(Yu and Gunasekaran, 2005b). Another aspect of cooker- continues unless it is interrupted by any material incompati-
stretcher design is the flight angle and pitch length of the ble with the protein matrix, such as fat globules, bacteria, or
screws. A larger flight angle (e.g., 45°) means less energy microparticulated fat replacers (McMahon et al., 1996). The
(SME) is input to the cheese mass, more energy is wasted mixing that occurs during the stretching, causes fat globules
and MRT increases (Yu and Gunasekaran, 2005b). There and most of the bacteria to be pushed together into increas-
is also less drag from the screw root and flights along the ingly smaller spaces until the fat globules are sufficiently
downstream direction leading to smaller flow and with the packed to physically inhibit fusion of the protein matrix.
decrease in SME, the exit temperature of the cheese drops. Thus, closely packed clusters of fat globules and bacteria
Yu and Gunasekaran (2005b) used variations in barrel are formed and oriented into channels between the parallel-
width/depth ratio to study pitch flight and observed that aligned network of protein fibers (Auty et al., 1999; Joshi
MRT increased but SME decreased as the width/depth ratio et al., 2004d; McMahon et al., 1999) as the molten LMMC
increased resulting in decreases in exit temperature. is extruded and molded into its final shape (Figs. 40.17
Yun et al. (1994) had observed that increasing the tem- and 40.18). The size and amount of fat-serum channels
perature of the cooking water from 57 to 74°C at a constant present in LMMC is dependent upon fat content rather than
screw speed decreased MRT and MSE, but sufficient heat moisture content. During stretching, excess moisture is tak-
was being transferred from the cooking water to the curd so en out of the cheese until the fat globules are closely packed
that the cheese exit temperature increased from 54 to 67°C. together, which results in the protein matrix being separated
The higher cook temperature resulted in less fat loss from into parallel strands.
the cheese and, interestingly, produced a firmer cheese with Plasticization of LMMC curd in the cooker/stretcher re-
a much more elastic network structure. These results could sults in loss of fat from the molten curd into the hot water.
be further enhanced since higher plasticization tempera- Such “cooker cream” needs to be harvested to minimize
tures result in greater inactivation of starter bacteria (Yun economic losses since it reduces cheese yield by up to 2%.
et al., 1995) and coagulant enzymes (Feeney et al., 2001) so There are techniques for making pasta-filata cheese without
less proteolysis will occur during storage. At cooker tem-
peratures ≥60°C, phase separation of fat and water occurs
so there is an optimal range for temperature and shear in
cooker/stretchers, which is dependent on composition (es-
pecially fat, moisture, protein-bound calcium) of the curd
being plasticized.
Kindstedt et al. (1995) observed that when screw speed
was varied while cooking water temperature was kept con-
stant at 74°C, lowering the screw speed increased both
MRT and cheese exit temperature. Cheeses that had the
higher exit temperature also had higher apparent viscosity
and firmness throughout storage, and higher levels of serum
could be expressed from the cheese upon centrifugation.
Less proteolysis occurred during storage of such cheeses,
and the amount of calcium in the expressible serum was
less than in cheeses that had a lower exit temperature during
FIGURE 40.17 Scanning electron micrograph of hot low-moisture
cooking/stretching. Kindstedt et al. (2004) proposed that ex- part-skim Mozzarella cheese after plasticization (fat has been re-
posure to higher temperatures as a result of hotter cooking moved during sample preparation).
FIGURE 40.18 Transmission electron micrograph of low-moisture part-skim Mozzarella string cheese. (Courtesy of Dr. Almut Vollmer, Western
Dairy Center, Utah State University, Logan, UT, USA).
using a hot water cooker/stretcher, and by adding other flow of another solute (Gerla and Rubiolo, 2003; Floury
components, such as starches, protein, fat, and emulsifying et al., 2009). If calcium levels in brine are low, calcium
salts, either before, during, or after the plasticization pro- is lost from the surface region of the cheese, allowing in-
cess (Dahlstrom et al., 2001; Gascolgne et al., 2002; Henry creased hydration and swelling of the casein matrix (Guinee
et al., 2006; Merrill and Anderson, 2007; Rhodes, 2000; et al., 2002; Joshi et al., 2004d) and a soft rind defect devel-
Thakar et al., 2002). ops (Kindstedt et al., 1996).
Increasing the calcium concentration to 0.4% in a
10% salt brine caused calcium-induced aggregation of
Brining proteins within Ragusano cheese, smaller pores, and sub-
In general, diffusion properties of cheese solutes depend sequent shrinkage of the cheese protein matrix (Fucà
upon the physicochemical characteristics, composition, et al., 2012). Such shrinkage as a consequence of high
and microstructure of the matrix (Floury et al., 2010; Luo calcium has been observed in a variety of cheeses (McMa-
et al., 2013), and the balance between protein–water and hon et al., 2005, 2009; Lu and McMahon, 2015; Pastorino
protein–protein interactions that determines the overall et al., 2003a). This shrinkage-induced flux of water out of
volume occupied by the fully hydrated cheese protein ma- the cheese could impede diffusion of Na+ and Cl− ions into
trix (McMahon et al., 2009). Salt penetration into cheese the cheese during the brining process (Fucà et al., 2012).
during brining has been described as an impeded diffusion Loss of moisture from the cheese pores caused by a high
process (Guinee, 2004). Permeability and diffusion of salt calcium level in brine appears greater than that caused by
into cheese is impeded by fat globules that block pores in high salt. Luo et al. (2013) found that the proportion of
the cheese matrix so salt penetration takes longer in cheeses bound water in LMMC decreased by 21% when 0.25% cal-
with higher fat (Fucà et al., 2012). cium was added to brine.
When a block of cheese is placed into brine (Fig. 40.12), Salt penetration into cheese during brining increases
there is a net movement of Na+ and Cl− ions from brine with temperature, which also promotes moisture loss and
into the cheese based on comparative compositions of both weight loss during brining (Melilli et al., 2006). Cheese can
cheese and brine (Guinee, 2004). There is also movement shrink or expand with changes in temperature implying that
of any ions, such as Ca2+ and H 2 PO−4 , into the brine if the protein matrix aggregation or protein solubilization are as
aqueous concentration is higher in the cheese than in the important as osmotic effects (McMahon et al., 2009), and
brine. When several solutes diffuse simultaneously, cross- can be attributed to the increased importance of hydropho-
diffusion, as well as the self-diffusion coefficient have to bic interactions at higher brining temperatures (Pastorino
be considered to account for the affect of one solute on the et al., 2002).
FIGURE 40.20 Scanning electron micrograph of low-moisture part-

skim Mozzarella cheese after 28 day of cold storage. (Reprinted from
Oberg, C.J., McManus, W.R., McMahon, D.J., 1993. Microstructure of
FIGURE 40.19 Scanning electron micrograph of cold low-moisture Mozzarella cheese during manufacture. Food Struct. 12, 251–258).
part-skim Mozzarella cheese after brining (fat has been removed dur-
ing sample preparation).
the fat globules, and the fat-serum channels have a honey-
comb appearance, and this process continues until the fat
Cheese Cooling and Storage
globules are completely encased within the protein matrix
When examining LMMC microstructure as it exits the (Fig. 40.20). Either the serum (along with any protein and
cooker/stretcher using scanning electron microscopy, the other water soluble components) has been absorbed into,
parallel fat/serum channels can be observed but the fat glob- and become an integral part of the protein matrix (Guo and
ules in the channels are lost during sample preparation and Kindstedt, 1995; Oberg et al., 1993), or the solubilized pro-
are not observed (Fig. 40.17) (Oberg et al., 1993). However, teins form a gel (Metzger et al., 2000). The amount of se-
after the cheese has been cooled and brined, the appearance rum expressible by centrifugation from LMMC decreases
of the protein matrix surface surrounding the fat-serum over the same time period (McMahon et al., 1999).
channels changes to having a dimpled texture with numer- The increase in protein hydration during the initial stor-
ous circular indentations (∼1–10 µm diameter) depicting age of LMMC (along with continued proteolysis) brings
the location and close-packing of fat globules (Fig. 40.19). about an improvement in cheese meltability. Unless other
Smaller circular and elliptical indentations (∼0.5–1 µm di- modifications to the chemical composition have been inten-
ameter) that correspond to the cocci starter culture are also tionally made, LMMC immediately after manufacture has
observed. The presence of fat globules in these channels poor meltability. This suggests there are relatively strong
can directly be observed using transmission electron mi- protein–protein interactions early in the aging process that
croscopy (Fig. 40.18). resist the tendency to flow when LMMC is heated, even
Based on these observations (Oberg et al., 1993), it ap- though expressible water and fat are present within the fat-
pears that the protein matrix presses upon the rigid com- serum channels. Thus, the presence of sufficient levels of
ponents contained within the fat-serum channels in cold free water and fat in the fat-serum channels is not enough
LMMC and surrounds the solidified fat globules and en- to ensure good meltability. As the proteins become more
trapped bacteria. These changes in microstructure and func- hydrated upon cooling and from salt addition (Paulson
tionality of LMMC during storage suggest proteins are not et al., 1998), some of the interactions between proteins are
in a quiescent state immediately after stretching and mold- replaced by interactions with bulk phase water molecules,
ing, but continue to undergo some structural rearrangement. enabling the proteins to flow more easily as the cheese is
During continued storage, fat globule impressions in the softened during heating, with melted fat having a lubrica-
protein matrix surface of the channel walls became more tion effect (Tunick et al., 1993). According to Lucey et al.
pronounced, changing from small indentations to large de- (2003), such flow takes place if bond-breaking events (or re-
pressions. By day 7 of storage, the protein matrix extends laxation) occur at the cross-linking points in the cheese pro-
from 0.5 to 1.0 µm into the fat-serum channels, so that the tein matrix. Conversely, adequate flow will not occur if the
spherical shape of the individual fat globules was distinctly activation energies required for protein disentanglements
defined. After 14 days, the protein matrix loosely surrounds and relaxation mechanisms are high (Meza et al., 2012).
During most of the cheesemaking process, the para- freezing and thawing, and have a narrower distribution
casein matrix of the renneted curd is dehydrated through (Kuo et al., 2003). This implies that access of water mol-
the action of cutting, agitation, heating, and acidification of ecules to exchangeable protons within the protein matrix
the curd. This can be attributed to hydrophobically-driven might be the dominant mechanism involved in water relax-
interactions between the proteins that further occur as the ation of frozen-thawed LMMC.
curd is heated in the cooker/stretcher. Cooling of LMMC to Unsalted fresh Mozzarella cheese freezes between −1
4°C changes cheese system thermodynamics as the impor- and −2°C whereas salted cheese freezes between −4 and
tance of hydrophobic interactions to free energy becomes −5°C (Ribero et al., 2007a). Thus, when LMMC is frozen,
negligible. As the proteins that constitute the network struc- the rate at which the temperature drops within the range of
ture became more hydrated, the hydrodynamic volume in- −1 to −7°C is critical to textural changes (Kuo et al., 2003).
creases so the protein matrix begins to extend into the spac- Rapid freezing preserved more stretch properties (an indi-
es between fat globules in the fat-serum channels. cation of protein–protein interactions) so shredding LMMC
Rate of proteolysis will vary, depending upon the before freezing is preferred, whereas thawing temperature
amount of residual coagulant in the cheese and the cheese had no effect (Oberg et al., 1992). Increased melting of
moisture content. Cheeses with higher moisture typically LMMC that has been frozen is consistent with some damage
undergo more rapid proteolysis. Altering the residual coag- occurring to the cheese microstructure (Kuo and Gunasek-
ulant level in the cheese up or down has a corresponding ef- aran, 2003). Formation of ice crystals along the fat-serum
fect on the rate of initial cleavage of the caseins. The extent channels in LMMC during freezing can cause ruptures along
of such proteolysis varies widely, depending upon cooker these channels, whereas in non-pasta-filata cheese, cracks
temperature and MRT during cooking/stretching, and the in the protein matrix occur (Kuo and Gunasekaran, 2009).
consequent thermal inactivation of the coagulant and starter During freezing, as liquid water in the cheese is convert-
cultures. Thermophilic starters used for LMMC survive and ed into ice crystals, there can be a slight loss of water from
remain metabolically active when the curd exit temperature the surface of shredded cheese. Even with a slow thawing
is low (∼55°C) (Petersen et al., 2000; Yun et al., 1995), process, not all of this water will be retained in the cheese
whereas using higher exit temperatures (62–66°C) will de- and, therefore must be accounted for when making the
crease starter survival and the amount of proteolysis that cheese. If the proper chemistry is attained during manufac-
occurs during subsequent storage (Kindstedt et al., 1995; ture of the cheese, the cheese can be cooled, shredded, and
Yun et al., 1994). Coagulant enzymes are inactivated more frozen on the day of manufacture (Barz and Cremer, 1993).
with higher plasticization temperatures, and such LMMC The advantage of frozen shredded LMMC is convenience
with limited residual coagulant activity will require a longer of use by pizza makers by increasing the shelf-life of func-
period of storage to develop desirable functional properties tional properties of the cheese.
than cheese that is stretched at a lower temperature. Con- Immersion freezing of LMMC in 23% (w/w) brine at
versely, such LMMC will have a longer shelf-life before it −15°C has been proposed as a means to combine freez-
becomes too soft for shredding, begins to melt excessively, ing and salt absorption (Ribero et al., 2007b; Zorrilla and
and loses stretch, elasticity and chewiness. Rubiolo, 2005a,b). For LMMC that has been stored frozen,
followed by thawing and refrigerated storage, there were no
differences observed in the microstructure of the cheeses
FREEZING compared to unfrozen cheese stored for the same time (Ri-
A way to prevent chemical, physical, and functional chang- bero et al., 2009). Such freezing did not appear to adversely
es in LMMC during storage is to freeze the cheese. Low- affect the cheese since maturation changes were halted by
moisture Mozzarella cheese can be frozen without the same freezing and then continued after thawing. Bertola et al.
extent of freeze-concentration and ice crystal formation that (1996) found that freezing LMMC after 14 days of refriger-
occurs during the freezing of high moisture soft cheeses, ated storage retarded changes in functionality so that when
which results in increased breakdown of the protein net- thawed after frozen storage, the aging process continued
work and increased maturation after thawing (Gravier from the time when it was frozen.
et al., 2004; Meza et al., 2011, 2012; Verdini et al., 2005).
When frozen LMMC is thawed, it has a slightly higher
water self-diffusion coefficient than before freezing, and CHEESE MICROBIOLOGY
this continues to increase with storage after thawing (Kuo
Starter Cultures
et al., 2003). This phenomenon is related to the microstruc-
ture of plasticized cheese as no such change occurs in non- Thermophilic LAB with optimum growth occurring be-
pasta-filata LMMC. The self-diffusion coefficient is higher tween 40 and 52°C are used as starter cultures for the man-
along the fat-serum channels than across the protein fibers. ufacture of pasta-filata cheeses, such as LMMC. This in-
The T2 relaxation times for water are slightly lower after cludes the lactobacilli (rods) Lb. delbrueckii ssp. bulgaricus
and Lb. helveticus, and the coccus S. thermophilus. If the are tightly associated with the bacterial cell wall, or secreted
mesophilic LAB, L. lactis, is used, then a lower cooking into the environment (sometimes as ropy masses of EPS).
temperature is required. Commercial starter cultures are The ability to produce EPS is highly variable in LABs, be-
carefully characterized, particularly for galactose utilization ing both strain-dependent and affected by the type of media
and for proteolytic capabilities. Galactose utilization can and growth conditions. Using capsular EPS cultures can
assist in predicting the effect of culture on cheese brown- increase cheese moisture content, especially in Mozzarella
ing during baking (Hutkins et al., 1986; Johnson and Ol- cheeses with lowered fat content, where they can help pro-
son, 1985). duce a softer cheese with increased melting (Broadbent
et al., 2001; Low et al., 1998; Perry et al., 1997, 1998; Zisu
and Shah, 2005, 2007). This occurs when the capsules sur-
Galactose Fermentation and Utilization
rounding the bacteria are large enough to physically restrict
Lb. helveticus, unlike Lb. delbrueckii ssp. bulgaricus, is able coalescence of protein strands, thus forming additional se-
to utilize the galactose moiety of lactose so there is less re- rum voids within the cheese matrix. There are also fewer
sidual galactose in the LMMC, resulting in less browning issues with carryover of EPS into the whey when capsu-
and blistering during cooking and baking on a pizza (Hutkins lar EPS cultures are used (Petersen et al., 2000), whereas
et al., 1986; Johnson and Olson, 1985; Oberg et al., 1991b). ropy EPS cultures can increase whey viscosity resulting in
The capacity to utilize both the galactose and glucose por- problems with processing operations, such as ultrafiltration
tions of lactose also accelerates acid drive in the vat. of whey.
When used as a bulk starter culture, rod, and coccus ther-
mophilic cultures are generally grown together with both
Proteolytic and Peptidolytic Activity
symbiosis and competition occurring to yield a particular
ratio of cocci to rods prior to vat inoculation. Rate of acid A diversity of proteolytic enzymes are found in thermo-
production in combined compatible coccus and rod cultures philic LAB, such as Lb. delbreuckii ssp. bulgaricus and Lb.
is greater than the sum of the acid production from the two helveticus, which results in different starter cultures pro-
single cultures (Barach et al., 1987; Marshall, 1987; White- ducing a unique variety of peptides and amino acids dur-
head et al., 1991). Lactobacilli degrade casein, supplying ing fermentation and aging (Oberg et al., 1991a,b, 2002).
peptides and amino acids to the weakly proteolytic strepto- S. thermophilus exhibits very little proteolysis compared to
cocci, which in turn produce formic acid and carbon diox- lactobacilli, but some strains may have atypical proteolytic
ide to stimulate growth of lactobacilli (Radke-Mitchell and activity. Mixed thermophilic cultures are also more pro-
Sandine, 1984; Thunell and Sandine, 1985). Coccus and rod teolytic than the sum of the individual cultures (Rajagopal
starter cultures can also be grown separately (Champagne and Sandine, 1990). The proteolytic specificity of different
et al., 1990; Thunell, 1986) although the lactobacilli (rods) starter culture strains can impact upon functional properties
tend to grow poorly on their own. Direct-to-vat starter cul- of LMMC, even when the overall proteolytic capacity is
tures are purchased separately as containers of either rods or similar (Oommen et al., 2002). Production of free amino
cocci, and can be added to the vat in a ratio according to the acids from cultures that exhibit high levels of proteolysis
preference of the cheese manufacturer. The coccus:rod ratio contributes to browning reactions, resulting in LMMC that
of starter cultures impacts upon the resultant properties of browns more when baked (Oberg et al., 1991a,b).
the LMMC (Whitehead et al., 1991; Yun et al., 1995). Use
of excess rods leads to increased proteolysis and a softer Bacteriophage
cheese body, whereas a higher ratio of cocci to rods (or
cocci only) produces cheese with slower maturation rates Many bacteriophages that attack thermophilic streptococci
(Oommen et al., 2002; Thunell and Sandine, 1985). Con- and lactobacilli have been isolated and characterized (Jar-
siderable variation amongst rates of acid production from vis, 1989), with the majority specific for S. thermophilus
carbohydrate fermentation were detected within subspecies (Barach et al., 1987; Rajagopal and Sandine, 1990). Bac-
(Sanders, 1991), as well as differences in proteolysis during teriophage attack during LMMC manufacture occurs more
storage (Oommen et al., 2002). frequently with long production schedules, leading to use
of culture rotations (Rasmussen, 1980; Thunell, 1989). In
addition, strategies have been developed to generate phage-
EPS-Producing Cultures insensitive strains (Mills et al., 2007). Although dead vats
A large number of exocellular polysaccharides (EPS) with are rare, slow acid production has a detrimental economic
various compositions and physical properties are pro- effect as it interferes with production schedules and plant
duced by thermophilic LAB, such as S. thermophilus and operations when making multiple vats of cheese each day.
Lb. delbrueckii ssp. bulgaricus (Broadbent et al., 2003; Failure of S. thermophilus from bacteriophage attack dis-
Cerning, 1990). Such EPS may be produced as capsules that rupts the growth synergism with the rod component in the
starter culture (Klaenhammer, 1989). As a consequence, CHEESE CHEMISTRY

S. thermophilus cultures are often rotated, like their meso-
philic lactococcal counterparts. However, unlike the com- Fat and Protein
plete stoppage of acid production that can occur in bacterio- Fat content of cheese has both a direct and an indirect influ-
phage-infected lactococcal starters during Cheddar cheese ence on cheese functional properties. During cheeesemak-
manufacture, acid production in LMMC manufacture will ing, because of the hydrophilic nature of the fat globule
continue in bacteriophage-infected lactobacilli until the in- membrane, there is no chemical interaction between the
fected cells lyse (Chow et al., 1988), so total inactivation fat globules and the protein. Instead, fat globules act as a
of the rod component during LMMC manufacture has not physical impediment to protein coalescence and become
been commonly reported. Bacteriophage can infect various entrapped within the shrinking protein gel network form-
strains of Lb. helveticus, however, since they are unrelated ing pockets containing fat globules and serum dispersed
to Lb. delbrueckii ssp. bulgaricus bacteriophage (Lahbib- throughout the cheese (Fig. 40.21B). When LMMC is made
Mansais et al., 1988), a rotation of rod species may be ad- with a reduced amount of fat, openness in the microstruc-
vantageous. ture is reduced. In nonfat cheese, no such fat/serum pockets
are formed (Fig. 40.21A), unless, for example, a micropar-
Cheese Microflora—Traditional ticulated ingredient is added that can interfere with protein
coalescence during cheesemaking (Fig. 40.22) (McMahon
Mozzarella Cheese
et al., 1996).
Most LMMC is made using defined starter cultures selected When LMMC curd is heated in the cooker/stretcher,
for rapid and consistent acid production that is required the protein–protein interactions increase due to increased
for large-scale manufacturing, however, there are various hydrophobic effects as temperature increases. Fat globules
traditional pasta-filata cheeses made using naturally oc- entrapped within the protein matrix act as noninteracting
curring LAB. Bacterial communities in cheeses produced fillers as the protein strands are aligned into parallel fi-
with raw-milk or natural starters are more complex (Mau- bers interspersed with serum-fat globule channels (Oberg
riello et al., 2003; Parente et al., 1997) and quickly change et al., 1993). Lowering the fat content of LMMC causes a
as the cheese ages (Morea et al., 1999). Starter cultures decrease in water-to-protein ratio in the cheese which af-
may involve naturally fermented whey from the previous fects LMMC functional performance more than the actual
day’s cheese manufacture, or may even come from use of moisture content of the cheese. Homogenization of milk
wooden cheese vats in which the LAB are from biofilms when fat is in the liquid state alters interactions between
on the wooden surfaces (Licitra et al., 2007). Rather than fat and casein and formation of the fibrous cheese matrix,
just containing S. thermophilus and Lb. delbrueckii ssp. therefore LMMC curds do not fuse together well, resulting
bulgaricus or Lb. helveticus, the microbial community of in poor melting (Van Hekken et al., 2007).
such cheeses can include other homofermentative and het- Fat acts as an inert filler in cheese when the temperature
erofermentative organisms, such as Lactobacillus planta- is high enough for milk fat to be liquid, and is dispersed
rum, Lactobacillus fermentum, Lactobacillus casei ssp. ca- throughout the protein matrix (Rogers et al., 2010). At cold
sei, Lactobacillus lactis, Weissella hellenica, Enterococcus temperatures, the solid fat globules provide a reinforcing
faecium, Leuconostoc mesenteroides subsp. mesenteroides, effect and the cheese acts as a filled gel. Increasing the fat
L. lactis, Streptococcus bovis, and Streptococcus uberis, content of cheese will produce a softer more pliable cheese
(Morea et al., 1998, 1999; Licitra et al., 2007; Parente because less volume is occupied by the protein matrix. When
et al., 1997; Piraino et al., 2008). Mesophilic bacteria, such cheese is heated, it is the fat portion that softens first, but the
as Ln. mesenteroides, do not generally survive during the extent of protein–protein interactions in the protein matrix
hot plasticization step of cheesemaking (Morea et al., 1999) actually determines flowability. Some cheeses with high lev-
so thermophilic LAB, such as S. thermophilus and Lb. del- els of protein–protein interactions, such as when calcium is
bruekii predominate after stretching, and then decline in retained at a high level, soften but do not flow when heated.
numbers during storage (Licitra et al., 2007). Because of Fat also plays an important role in melting of LMMC
the genetic diversity in such raw milk or “traditional” pasta- when cooked on a pizza in forced-air convection ovens. This
filata cheeses made with LAB exhibiting wide variations in type of heating exposes cheese to an environment that rap-
acid production and proteolytic ability, isolates from such idly causes evaporation of moisture from the surface of the
cheese systems may have application as starters or adjuncts shredded cheese. Release of fat onto the surface of shred-
in larger commercial operations (Piraino et al., 2008). Com- ded cheese retards evaporation, which allows the cheese to
bining a fast acid producing culture with cultures with mod- melt and flow before the surface is dehydrated and browns.
erately high general peptidase activity could allow manu- The melt of nonfat Mozzarella cheese on a pizza can be
facture of cheeses with different functional properties or improved by spraying the cheese surface with a thin coat
flavor development. of oil (Rudan and Barbano, 1998; Zaikos et al., 1999) or
FIGURE 40.21 Scanning electron micrograph of (A) nonfat Mozzarella cheese and (B) part-skim Mozzarella cheese sectioned perpendicular to the
protein strands showing lack of presence of fat/serum channels between protein strands in nonfat cheese.
structuring the cheese so the fat can be more easily released Ren et al. (2013) made LMMC from the milk of Hol-
onto the cheese shred surface (Wadhwani et al., 2012). A stein cows that had different genetic k-casein polymorphs
similar effect can also be observed if other condiments that (AA, AB, AE, or BE) and found that LMMC made from
release either fat (e.g., pepperoni) or moisture (e.g., green type AB milk was harder, chewier, and had higher stretch-
peppers) are placed on top of the shredded cheese before ability but lower meltability than LMMC made from either
the pizza is baked. type AE or BE milk. This finding was attributed to k-casein
AB milk having the highest calcium content, so the LMMC
produced had a higher calcium/protein ratio and lower
moisture. Increased calcium promotes more protein–protein
interactions in the cheese so that the proteins maintain self-
association and have low adhesiveness and would have less
melt and more stretch.
Proteolysis
Proteolysis of caseins begins during curd formation, then
continues through refrigerated storage of the cheese.
Changes in stretch and melt of LMMC have been associ-
ated with proteolysis during aging (Oberg et al., 1991a,b)
including specificity of bacterial proteases produced by
starter cultures (Oommen et al., 2002). Proteolysis in
LMMC increases with increased moisture content (Tunick
and Sheih, 1995). In most bacteria-ripened cheeses, the
first casein to be hydrolyzed is αs1-CN, with little initial
enzymic cleavage of β-casein and para-k-casein (Nauth
and Ruffie, 1995). Plasmin and chymosin both contribute
FIGURE 40.22 Scanning electron micrograph of low-fat Mozza- to the production of peptides during proteolysis (Malin and
rella cheese in which microparticulated fat replacer has been added.
Brown, 1995), providing substrates for starter culture pro-
(Reprinted with permission from McMahon, D.J., Alleyne, M.C., Fife,
R.L., Oberg, C.J., 1996. Use of fat replacers in low-fat Mozzarella cheese. teases and peptidases to produce peptides and amino acids
J. Dairy Sci. 79, 1911–1921). necessary for bacterial metabolism. The extent of proteolysis
in LMMC has been measured in various studies with levels chymosin rather than bovine chymosin is used for making
of intact αs1-casein remaining after 28 days storage ranging LMMC (Moynihan et al., 2014). LMMC made using camel
from 64% (Stone, 1999) to 50% (Kiely et al., 1993) to 25% chymosin remains firmer and retains a chewier texture dur-
(Farkye et al., 1991; Fife et al., 1996). Hydrolysis of αs1- ing extended storage, and when baked on a pizza, the cheese
casein can also be followed by observing the appearance maintains blister quantity, strand thickness, hardness, and
of breakdown peptides, such as αs1-casein (f24–199) upon chewiness. Other methods for extending the storage period
hydrolysis by chymosin. This large peptide has been report- when LMMC has optimum melt and stretch properties in-
ed as comprising up to 24% of the total α- and β-caseins clude using preacidification of milk prior to renneting so
in LMMC after 6 weeks of storage (Tunick et al., 1993). less rennet is needed, and using only S. thermophilus as the
When high cooking temperatures (e.g., 46°C) are used dur- starter culture without Lb. helveticus or Lb. delbruekei ssp.
ing curd manufacture, there is less residual chymosin activ- bulgaricus.
ity, less proteolysis and αs1-casein (f24–199) levels drop
to ∼10%. Continued proteolysis results in smaller peptide
fragments being formed by the action of residual coagu- Calcium and Moisture
lant, plasmin, and enzymes from nonstarter bacteria (Dave Calcium ions, because of their ability to ionically bind to neg-
et al., 2003b). Melting of LMMC better correlates to loss of atively-charged groups on proteins, as well as to phosphate
intact β-casein (R2 = 0.72) and extent of overall proteolysis, ions, play an important role in promoting protein–protein
measured as soluble nitrogen (R2 = 0.76) than it does to interactions in cheese and therefore strongly affect cheese
loss of intact αS1-casein (R2 = 0.36) (Dave et al., 2003b). functionality (Joshi et al., 2003; Paulson et al., 1998; Pasto-
Changes in melting during storage also appear to follow the rino et al., 2003a). Variations in calcium content accounts
trend lines for combined loss of αS1-casein and αS1-casein for 50% or more of the variation in melting and flow proper-
(f24–199) (Dave et al., 2003a). When chymosin is used ties of Mozzarella cheese (Joshi et al., 2004c). Cheeses with
as a coagulant, there is little hydrolysis of β-casein (Kiely reduced calcium levels (e.g., 0.3%) have higher moisture,
et al., 1993) compared to a 40% decrease in intact β-casein are softer, have lower elastic and viscous moduli, increased
over 29 days of storage when using coagulant from Crypho- meltability and stretchability (Joshi et al., 2004a,b; Pasto-
nectria parasitica (Farkye et al., 1991). The protease from rino et al., 2003a; Rehman and Farkye, 2006). This occurs
C. parasitica is more proteolytic and has greater specificity because as protein–protein interactions decrease, protein
for β-casein compared to chymosin, which has more speci- hydration increases, which means more whey remains en-
ficity towards αs-caseins (Yun et al., 1993). In direct-acid trapped within the protein matrix (Guinee et al., 2002; Joshi
LMMC, Dave et al. (2003b) reported a 50% loss of intact et al., 2004d; McMahon et al., 2005). Conversely, inject-
β-casein over 15 days made using C. parasitica coagulant. ing calcium directly into cheese causes the protein fibers
The type of coagulant has less effect on firmness of in the cheese matrix to contract and expel whey (Pastorino
LMMC (Dave et al., 2003b). It may be that αS1-casein (f24– et al., 2003a). Observed effects of pH on cheese function-
199) imparts the same structural and functional properties ality are a consequence of changes in calcium phosphate
to the cheese protein matrix as does intact αS1-casein. It has solubility (Pastorino et al., 2003b). So when less calcium is
been suggested that αs1-casein (f121–199) may be pres- bound to the casein, the protein matrix becomes more hy-
ent during aging of cheese at higher levels than αS1-casein drated and the cheese melts more easily. Above pH 5.0, mi-
(f24–199), and that the ratio of αs1-casein (f121–199) to in- crostructure, texture, and meltability of cheese is dependent
tact αs1-casein may be a useful predictor of aging (McMa- upon calcium content rather than pH. At pH < 5.0, loss of
hon et al., 2014). casein solubility because of pH becomes the predominant
Less proteolysis occurs when LMMC is plasticized factor affecting cheese functionality, and cheeses loses the
at higher cooker/stretcher exit temperatures (Renda ability to melt and stretch, even with reduced calcium con-
et al., 1997). More proteolysis occurs when cheese is made tent (Ge et al., 2002; Pastorino et al., 2003b).
using direct acidification as partitioning of chymosin be- Interaction of positively charged calcium ions with neg-
tween curd and whey is 85:15 at pH 5.2, whereas at pH atively charged regions of caseins can lead to neutralization
6.6 it is 30:70 (Holmes et al., 1977). Only ∼6% of coagu- of charge repulsion between the caseins, as well as con-
lant added to milk is retained and active in cheddar cheese, tribute to bridging between proteins to produce a stronger,
and further losses would be expected during cooking more cross-linked protein matrix (Pastorino et al., 2003a).
and stretching in the manufacture of LMMC. Dave et al. In contrast, monovalent ions, such as sodium, have a slight
(2003b) observed 40% hydrolysis of αs1-casein after 1 day salting-in effect at low concentrations making the proteins
in a direct acid LMMC, with 90% hydrolyzed after 17 days. more soluble and a salting-out effect at high concentra-
When the coagulant level was reduced fourfold, there was tions making them less soluble (Paulson et al., 1998). Al-
a corresponding fourfold decrease in the rate of hydrolysis though electrostatic interactions (and hydrogen bonding)
during storage. Slower proteolysis also occurs when camel between proteins take place within the cheese matrix, these
are independent of calcium crosslinking, and only when calcium, a salting-in effect on protein solubility, and loss
the cheese matrix is depleted of calcium are the proteins of hydrophobically-induced interactions. After manufac-
released from each other (Gagnaire et al., 2002). Hence, ture, up to 50% of the water in LMMC can be expressed
cheeses with high calcium content have poor melting and by centrifugation (Guo and Kindstedt, 1995; McMahon
flow properties. et al., 1999) and this is considered an indicator of the lack of
Moisture will migrate into or out of the protein matrix water-holding capacity of the cheese (Guinee et al., 2002).
based on both the chemical environment surrounding the During cold storage, the amount of expressible serum de-
proteins and cheese temperature (Pastorino et al., 2002). creases to zero after about 14 days as the protein matrix be-
The direction of serum movement depends upon whether comes fully hydrated and entraps the remaining bulk water.
the free energy of the total system (protein plus surrounding Applying high pressure to cheese soon after manufacture
aqueous phase) can be lowered by the proteins becoming accelerates protein hydration, and the change in protein mi-
more or less hydrated through protein–protein aggregation. crostructure is evident with a loss of cheese opacity (John-
Thus, in cheeses with a high calcium content, the system fa- ston and Darcy, 2000; Sheehan et al., 2005). Sheehan et al.
vors low protein hydration (with increased protein–protein (2005) did not observe any changes in rheological proper-
interactions) so the proteins exist as densely compacted pro- ties or melt and stretch of high pressure-treated reduced fat
tein bundles with less moisture contained within the protein Mozzarella cheese, but Johnston and Darcy (2000) reported
matrix and more moisture being present as free serum pock- a tendency for high pressure treated reduced fat Mozzarella
ets (Fig. 40.23). Calcium mediated crosslinking of proteins to have less tendency to fracture, increased plasticity and
leads to increased structural rigidity of the cheese matrix softness, and less fines during shredding.
and increased cheese hardness (Joshi et al., 2004b; Pastori-
no et al., 2003a; Sheehan and Guinee, 2004) and decreased Salt and Sodium
melt performance (Guinee et al., 2002; Joshi et al., 2004c,d;
Sheehan and Guinee, 2004). Conversely, as calcium is Saltiness is one of the most important flavor attributes
lowered, protein–protein interactions within the protein of cheese (Liem et al., 2011) and is directly correlated to
matrix decrease while protein–water interactions increase. overall desirability by consumers (Schroeder et al., 1988).
Thus, it becomes thermodynamically favorable for water A slight decrease in consumer liking of part-skim LMMC
to diffuse into the protein matrix and the overall protein occurs with a 25%–33% salt reduction followed with a
matrix becomes more hydrated (Guinee et al., 2002; Joshi further decrease in liking at 50% salt reduction (Ganesan
et al., 2004d; McMahon et al., 2005). The fibrous structure et al., 2014). As well as a drop in salty flavor, they reported
characteristic of pasta-filata cheeses (Figs. 40.1, 40.17– decreased levels of brothy, buttery, lactone/fatty acid, sul-
40.18) requires partial calcium solubilization so the protein fur, umami, and sour flavors (even though cheese pH was
matrix can deform and flow in the cooker/stretcher while the same). Likeability scores remained higher when the
retaining some protein–protein interactions. reduced-salt cheeses were consumed baked on a pizza. No
Some water molecules in cheese can be considered differences in texture or flavor was observed when NaCl
bound to proteins and occupy interstitial protein spaces, was replaced with up to 75% KCl during the manufacture
or are hydrodynamic layers of water that surround the pro- of LMMC (Ayyash and Shah, 2011; Ayyash et al., 2013).
tein surface (McMahon et al., 1999). Such water molecules
are not available as a solvent and exhibit slower rotational CHEESE FUNCTIONALITY
and translational speeds than bulk water molecules (Farrell
et al., 1989). Bulk water can be divided into entrapped or
Rolling
free water, depending upon the mobility within the protein Mozzarella cheese possesses yield stress and shear-thin-
matrix. Water that is impeded or entrapped within the mac- ning behavior under shear flow that can be described by
rostructure of the cheese protein matrix is not expressed by the Herschel–Bulkley model of viscoplasticity (Mitsoulis
centrifugation (McMahon et al., 1999). Thus, the distribu- and Hatzikiriakos, 2009). This allows LMMC to be shaped
tion and movement of water in LMMC may be character- by rolling, provided the reduction is relatively small so as
ized as being either bound to proteins, entrapped by the pro- to maintain structure and appearance of the cheese (Mu-
tein matrix, or expressible by centrifugation. liawan and Hatzikiriakos, 2008). Greater reductions can be
During most of the cheesemaking process, the protein obtained at higher temperatures when the LMMC is in a
matrix of renneted curd is dehydrated through the action molten state. The cheese can be rolled cleanly at 25°C with-
of cutting, agitation, heating, and acidification of the curd. out any significant adherence of cheese on the rollers. The
This is reversed during cold storage. Changes in micro- exiting sheet thickness increases appreciably with increas-
structure of LMMC during cold storage (Figs. 40.19–40.20) ing roll speed and entry thickness, as does the torque. This
can be explained by water moving into the protein matrix rolling process is essentially isothermal. Unyielded regions
in response to solubilization of some of the protein-bound are limited to the incoming and outgoing sheets leaving all
FIGURE 40.23 Transmission electron micrograph of nonfat Mozzarella cheese containing 0.6% (top) and 0.3% (bottom) calcium. (Reprinted
with permission from McMahon, D.J., Paulson, B.M., Oberg, C.J., 2005. Influence of calcium, pH and moisture on protein matrix structure and function-
ality in direct acidified nonfat Mozzarella cheese. J. Dairy Sci. 88, 3754–3763).
material yielded between the rolls, as opposed to extrusion, of shredded cheeses in the USA dominated the retail mar-
in which some unyielded regions of viscoplastic fluids can ket and grew 3.5% to $4.2 billion (Kennedy, 2013). Shred-
remain (Mitsoulis et al., 1993). ded LMMC is also sold in the food service market in both
refrigerated and frozen form. Cheese shreds need to be
uniformly and precisely cut to meet individual customer
Shredding expectations. Often during handling, distribution, and stor-
In most cases, LMMC is shredded for use in food applica- age, shreds can crumble, stick, or mat (Hongxu and Guan-
tions and this can occur immediately prior to use, or more sekaran, 2004). To prevent caking or stickiness, an anticak-
frequently, LMMC is sold in shredded form. In 2013, sales ing agent, such as powdered cellulose or starch is added
to the shredded cheese. Typically, LMMC does not shred In contrast, Banville et al. (2013) observed only a minor
well until it has been stored long enough for hydration of trend of fines with temperature. Lower calcium content in-
the protein matrix to occur (∼4–5 days), but if aged for too creases cheese adhesion to the cutting blade when LMMC
long (over ∼20 days), it loses firmness and also does not is shredded at 22°C (Banville et al., 2013). At lower tem-
shred well. Any conditions that soften the cheese, such as peratures (4 and 13°C) the cheese residue on the cutting
too high moisture content, will make it more difficult to blades is particulate, whereas at 22°C, it spreads over the
shred or slice. Conversely, if LMMC is too firm and dry, blades. Longer storage times before shredding tend to cause
it may shatter into small pieces during shredding causing more adhesion of cheese to the cutting blades, and good
yield losses during conversion and dissatisfaction by the shreddability is not restored by shredding older LMMC at
user (Dubuy, 1980; Kindstedt, 1995). colder temperature (Chen, 2003).
Shreddability of cheese takes into account the ease with Matting of LMMC after shredding increases with tem-
which a block of cheese is shredded, length, and integrity of perature since cohesion strength increases, softening of the
shreds, propensity of shreds to remain free flowing or mat cheese promotes higher compaction into a cake, and partial
together after shredding, and the propensity of shredded melting of milkfat releases free oil on the shred surfaces that
particles to shatter into fines either during or after shred- solidifies during cooling (Banville et al., 2013). Breaking of
ding (Childs et al., 2007; Kindstedt, 1995). Shredding may the cakes of matted cheese also increases with temperature,
also produce shreds with ragged edges, many fines, gum- such that at 22°C, they fracture into bigger clumps and re-
my balls of cheese, and excessive matting. Ideally, cheese quire more force to fracture than at 4°C where the cakes are
shreds should be cut uniformly and precisely, which allows puffy and light and fall apart easily (Banville et al., 2013).
the cheese to melt evenly and easily (Dubuy, 1980) and re- Having matted shreds break apart easily facilitates shred
tain these characteristics during handling, distribution, and handling and distribution (Kindstedt, 1995).
storage (Ni and Gunasekaran, 2004). Childs et al. (2007)
found that factors regulating rheological and surface tack Melting and Stretching
properties of cheese are important to the shredding qual-
ity. Specifically, tack energy (although not surface energy) An important functional property of LMMC when used as a
and a decrease in retardation time were correlated with pizza topping and in various other food formulations, is the
adherence to the blade, and fines were associated with in- ability to melt yet retain stretch (Fife et al., 1996; Gunasek-
creased initial and maximum compliance (i.e., the cheese aran and Ak, 2003). Sufficient melting and flow of LMMC
being more deformable). There are commercial processes in shreds during pizza baking is needed to form a continuous
which Mozzarella cheese can be shredded immediately after mat of melted cheese without any obvious presence of indi-
manufacture (within 2 h after brining and cooling) although vidual cheese particles. The softening or transition tempera-
the cheese has to be used within 48 h or frozen (Barz and ture is the temperature at which cheese just begins to flow
Cremer, 1993). Another approach to making cheese shred- under constant force when heated and represents the ease
dable without prior storage is through high pressure pro- of melting of a cheese (Muthukumarappan et al., 1999).
cessing (300–500 MPa) as shown by Serrano et al. (2004) in Stretching refers to the ability of a cheese to elongate un-
which acceptable shredding of cheddar cheese was obtained der load when heated, with formation of fibrous strands of
after just 1 day of storage. melted cheese that extend under tension (Fife et al., 2002;
Production of fines during shredding of LMMC can be Gunasekaran and Ak, 2003; Kindstedt, 1995).
related to the fibrous structure. At the typical storage time Various empirical methods for measuring the extent of
when LMMC is shredded, there are still channels of free se- cheese melting have been developed, as well as different
rum and fat that act as lines of weakness, and the cheese is rheological tests, and these have been reviewed by Kindst-
brittle (Banville et al., 2013). Such heterogeneity can pro- edt et al. (2004). Meltability of LMMC has been described
mote microcrack formation since applied stresses are then as the distance a sample of cheese flows when heated, or the
distributed unequally across the cheese matrix (Gunasekaran decrease in height when it is tested under specified condi-
and Ak, 2003). Calcium-mediated protein–protein interactions (Ma et al., 2011). Using small amplitude oscillatory
tions contribute to the fibrous structure, and as LMMC ages, shear analysis (Ma et al., 2011) found that the transition
the free serum in fat/serum channels is absorbed into the temperature when G″ becomes greater than G′ varied only
protein matrix so weak points for microcrack formation are ∼3°C between cheeses that had different extents of flow
diminished. Fines production during shredding can be de- when heated. It has been proposed that an activation energy
creased by lowering the calcium content of cheese by ren- for cheese melting could be determined using complex vis-
neting at a lower pH during manufacture of LMMC (Ban- cosity (η*) as a measure of resistance to flow, and plotting ln
ville et al., 2013). Childs et al. (2007) reported an increase η* versus inverse of temperature (between 30 and 45°C) us-
of 71% in fines when shredding temperature was increased ing the Arrhenius equation (Dimitreli and Thomareis, 2004;
from 12 to 20°C, associated with a more deformable cheese. Tunick, 2010). Such activation energy is a reflection of the
energy needed to break down the cheese structure and allow correlation to the pizza fork test could be obtained. Mea-
flow (Ma et al., 2011). surements of load can differentiate between melted cheeses
When other parameters (such as fat content, calcium that remain too elastic (high maximum load) from those
levels, extent of proteolysis, and storage time) are held that have lost elasticity (low maximum load) even though
constant there is a correlation between moisture content of they may have similar pizza fork test values. Similarly, a
LMMC and meltability (Perry et al., 1997). With higher cheese where high maximum load occurs with low exten-
moisture, less energy is needed to release water from the sion, is indicative of a low-fat Mozzarella cheese with low
protein matrix to act as a plasticizer, and thus cheese melts meltability and no stretch (i.e., fork test value ≤3 cm) or a
more easily, and has a lower softening temperature (Ma LMMC that has not been aged sufficiently to develop opti-
et al., 2013b). Cheese that melts at a lower transition tem- mum melting and stretch properties.
perature has a longer time to flow and form blisters, and Ma et al. (2012) carried out stretching of cheese inside
thus bigger blisters on the baked pizza can be produced (Ma a column of temperature-controlled oil to eliminate tem-
et al., 2013b). Calcium content has a large effect on melting, perature and humidity fluctuations compared to stretching
and LMMC made using direct acidification has the same cheese in ambient air. Their stretch profile can be divided
meltability immediately after manufacture as LMMC made into two regions beginning with, (1) the load increasing as
using cultures and stored for 28 days (Rehman et al., 2003). the hook traverses the reservoir of molten cheese followed
Proteolysis during storage decreases protein–protein inter- by a rapid decrease during this unstable deformation pe-
actions, so when cooker/stretcher temperatures are lowered, riod as the hook leaves the cheese reservoir, and (2) as the
coagulant enzyme and starter culture remain at higher lev- cheese forms a stable neck and the rate of the change in load
els, producing softer LMMC with increased melting (Ma decreases. The second region starts at the inversion point,
et al., 2013a; Tunick and Van Hekken, 2006). when the stable neck has formed and the load gradually in-
There have been various analytical tests developed in creases until the end of the test. Stretching in an oil environ-
the past to measure stretching (Ak et al., 1993; Apostopou- ment differs from stretching cheese in ambient air where the
los, 1994; Ak and Gunasekaran, 1995; Fife et al., 2002; cheese cools, dehydrates and hardens as it is extended (Fife
Guinee and O’Callaghan, 1997; Kindstedt et al., 1989) as et al., 2002). The slope of the decrease as the hook egresses
an alternative to the pizza fork test (USDA, 1980). These the cheese mass (the unstable deformation region) is also
have either used custom built equipment, or sample hold- a useful parameter that can be correlated with the pizza
ers for various commercially manufactured tensile testers. fork test (Moyes, 2003), and relates to the formation of a
However, the pizza fork test is still commonly used for stable neck in polymer stretching (Nazarenko et al., 1994).
evaluating LMMC functionality by cheese manufacturers Another method to evaluate stretchability of cheese that
and the pizza industry even though it suffers from large op- avoids temperature and humidity variability is based on the
erator variations. As well as the overall length of stretch ring-and-ball method used to measure the softening point of
before the strand breaks, visual observations are made on polymers (Hicsasmaz et al., 2004). Stretch length could be
shred identity (continuous mass of melted cheese versus used to discriminate between LMMC of different ages and
observable individual shreds) and on the quantity and con- was further used to estimate extensional viscosity. There
sistency of the cheese pulled up by the fork during the test. is a still a need to develop a convenient, easily available,
A low fork test value can result from the LMMC having reproducible method to measure stretch.
strong protein–protein interactions (such as occurs in young
cheese), insufficient calcium solubilization, or at the other Baking, Browning, and Blistering
extreme, insufficient protein–protein interactions (such as
in LMMC that has been stored for too long, e.g., 60 days The generally preferred appearance for Mozzarella cheese
or more). Thus, there continues to be further method de- when baked on a pizza is for the formation of brown blis-
velopment on obtaining quantitative data suitable for sci- ters spread evenly over the white/yellow surface of the
entific investigation of the material processes taking place cheese rather than a general browning. Such blister forma-
during the stretching process (Hicsasmaz et al., 2004; Ma tion can be evaluated by measuring the size and the shape
et al., 2012; Moyes, 2003). of cheese blisters on pizza, and browning can be quanti-
Moyes (2003) studied various parameters from a load- fied using computer visioning (Ma et al., 2013b; Wang and
extension (stretch) profile, based on Fife et al. (2002), Sun, 2001, 2003). Wang and Sun (2001) found that slight
in which a three-pronged metal hook is raised through a browning occurs when LMMC reaches 70°C and then in-
mass of melted cheese. Using various parameters, such as creases only slightly with further increase in temperature.
maximum load as the hook traverses through the mass of Interestingly, Wang and Sun (2003) observed that LMMC
melted cheese (80°C), the extension at which maximum became whiter upon initial baking and then darkened as
load occurs, the extension when the load reaches a baseline Maillard reactions occurred between reducing sugars and
value, and the load at a fixed extension, a multiple linear amino compounds in cheese (Thomas, 1969), producing
brown coloration. Such whitening of Mozzarella cheese produce lactic acid, so residual galactose remains in the
upon heating has been reported by others (Dave et al., 2001; cheese unless it is metabolized by other bacteria. More
Metzger et al., 2000, 2001; Pastorino et al., 2002). browning occurs if Lb. delbrueckii ssp. bulgaricus is used
Overall browning of LMMC is independent of mois- because it does not ferment galactose, whereas Lb. helve-
ture content and depends upon galactose levels (Johnson ticus cultures can ferment galactose (Oberg et al., 1991a).
and Olson, 1985) and extent of proteolysis. However, Using strains of S. thermophilus that can utilize galactose
blisters become larger with higher moisture in LMMC be- and not release it into the curd will produce cheese with
cause of more steam being produced during heating (Ma less browning (Matzdorf et al., 1994). Cheeses made from
et al., 2013b). Large blisters are usually less circular than strains of Lb. helveticus that have more proteolytic ability
smaller blisters, and cheeses with lower elasticity or stretch- have more browning (Oberg et al., 1991a,b), as the sec-
ing resistance can form larger blisters (Ma et al., 2013b). ond component required for browning is the concentration
Cheeses with higher salt have smaller blisters and this was of available amino groups. During refrigerated storage of
thought to relate to the softening temperature increasing at LMMC, proteolysis produces one more free amino group
higher salt levels. for each peptide bond hydrolyzed. If LMMC is made using
Blisters are trapped pockets of heated air and steam chemical acidification without starter cultures, there is little
that become preferentially scorched during baking. When proteolysis and little browning occurs (Oberg et al., 1991a).
shredded LMMC is baked on a pizza base, as the shreds Since most S. thermophilus cultures have very little proteo-
begin to melt and fuse with each other, some fat globules lytic ability, using a coccus-only starter culture minimizes
melt and are released from the protein matrix to form free changes during storage that result from proteolysis (such
oil that covers the cheese surface. Such expressed oil im- as browning), as well as providing a longer shelf-life for
pedes moisture loss from the cheese. Moisture in the cheese the cheese (because the cheese stays firm for longer) before
is converted into steam during heating, and the expanding sale in the food service industry.
steam lifts the cheese around it against the internal elastic
and stretching resistances of the cheese (Ma et al., 2013b). REFERENCES
The force of the steam increases as more water evaporates,
Ak, M.M., Gunasekaran, S., 1995. Measuring the elongational properties
whereas the elastic and stretching resistances decrease as
of Mozzarella cheese. J. Texture Stud. 26, 147–160.
the temperature increases. A gas pocket grows bigger until
Ak, M.M., Bogenrief, D., Gunasekaran, S., Olson, N.F., 1993. Rheological
there is a balance between the force of the steam and the evaluation of Mozzarella cheese by uniaxial horizontal extension. J.
elastic and stretching resistances of the cheese. As free oil Texture Stud. 24, 437–453.
flows from the top of each bubble to the bottom, moisture Apostopoulos, C., 1994. Simple empirical and fundamental methods to
evaporates much more easily from the top. Thus, scorching determine objectively the stretchability of Mozzarella cheese. J. Dairy
occurs at the top of bubbles, which is recognized as blisters. Res. 61, 405–413.
Since the force of the steam has to overcome the elastic Auty, M.A.E., Fenelon, M.A., Guinee, T.P., Mullins, C., Mulvihill,
and stretching resistances of the cheese, smaller bubbles are D.M., 1999. Dynamic confocal scanning laser microscopy methods
formed in cheese with higher modulus, or with lower mois- for studying milk protein gelation and cheese melting. Scanning 21,
ture content. Free oil modulates cheese dehydration and af- 299–304.
Ayyash, M.M., Shah, N.P., 2011. The effect of substitution of NaCl with
fects cheese browning during baking (Richoux et al., 2008;
KCl on chemical composition and functional properties of low-mois-
Rudan and Barbano, 1998), and different amounts of free
ture Mozzarella cheese. J. Dairy Sci. 94, 3761–3768.
oil may be produced by Mozzarella made with different Ayyash, M.M., Sherkat, F., Shah, N.P., 2013. Effect of partial NaCl
starter cultures (Ma et al., 2013a). Lower fat Mozzarella substitution with KCl on the texture profile, microstructure, and
cheeses have insufficient fat to release onto the cheese sur- sensory properties of low-moisture Mozzarella cheese. J. Dairy
face to prevent dehydration, so spraying the cheese surface Res. 80, 7–13.
with a thin coat of oil prior to baking reduces dehydration Bähler, B., Hinrichs, J., 2013. Characterisation of Mozzarella cheese
(Rudan and Barbano, 1998). Alternatively, if fat is added curd by means of capillary rheometry. Int. J. Dairy Technol. 66,
to cheese curd pieces after the curd is formed, then a lower 231–235.
fat cheese can be manufactured in which the fat is released Banville, V., Morin, P., Pouliot, Y., Britten, M., 2013. Physical properties
more easily during heating so that it coats the surface of the of pizza Mozzarella cheese manufactured under different cheesemak-
ing conditions. J. Dairy Sci. 96, 4804–4815.
cheese (Wadhwani et al., 2012).
Barach, J.T., Talbott, L.L., Leonhard, P.J., 1987. Starter strain charac-
The presence of a reducing sugar in cheese is critical
terization for an Italian DDS culture program. Proc. 24th Annual
for browning to occur. This can come from residual lactose Marschall Italian Cheese Seminar, Madison, WI, USA, pp. 17–29.
or galactose after cheesemaking, or when ingredients, such Barz, L.B., Cremer, C.P., Durkin, A.V., 1999. Process of making a soft of
as skim milk powder are added to the hot cheese as part of semi-soft fibrous cheese. US Patent 5,902,625.
the cooking/stretching process (Barz et al., 1999). S. ther- Barz, R.L., Cremer, C.P., 1993. Process of making acceptable Mozzarella
mophilus only utilizes the galactose portion of lactose to cheese without aging. US Patent 5,200,216.
Bertola, N.C., Califano, A.N., Bevilacqua, A.E., Zaritzky, N.E., 1996. Fife, R.L., McMahon, D.J., Oberg, C.J., 2002. Test for measuring the
Textural changes and proteolysis of low-moisture Mozzarella cheese stretchability of melted cheese. J. Dairy Sci. 85, 3539–3545.
frozen under various conditions. Lebensm.-Wiss. u.-Technol. 29, Floury, J., Jeanson, S., Aly, S., Lortal, S., 2010. Determination of the dif-
470–474. fusion coefficients of small solutes in cheese: a review. Dairy Sci.
Broadbent, J.R., McMahon, D.J., Oberg, C.J., Welker, D.L., 2001. Use of Technol. 90, 477–508.
exopolysaccharide-producing cultures to improve the functionality of Floury, J., Rouaud, O., Le Poullennec, M., Famelarta, M.H., 2009. Reduc-
low fat cheese. Int. Dairy J. 11, 433–439. ing salt level in food: part 2. Modelling salt diffusion in model cheese
Broadbent, J.R., McMahon, D.J., Welker, D.L., Oberg, C.J., Moineau, S., systems with regards to their composition. LWT Food Sci. Technol.
2003. Biochemistry, genetics and applications of exopolysaccharide 42, 1621–1628.
production in Streptococccus thermophilus: a review. J Dairy Sci. 86, Francolino, S., Locci, F., Ghiglietti, R., Iezzi, R., Mucchetti, G., 2010.
407–423. Use of milk protein concentrate to standardize milk composition in
Cerning, J., 1990. Exocellular polysaccharides produced by lactic acid Italian citric Mozzarella cheesemaking. LWT Food Sci. Technol. 43,
bacteria. FEMS Microbiol. Rev. 87, 113–130. 310–314.
Champagne, C.P., Brouillette, M., Girard, F., 1990. Effect of maturity of Fucà, N., McMahon, D.J., Caccamo, M., Tuminello, L., La Terra, S.,
Lactobacillus delbrueckii subsp. bulgaricus cultures on growth of Manenti, M., Licitra, G., 2012. Effect of brine composition and brin-
Streptocoocus salivarius subsp. thermophilus. Can. Inst. Food Sci. ing temperature on cheese physical properties in Ragusano cheese. J.
Technol. J. 23, 203–206. Dairy Sci. 95, 460–470.
Chen, C., 2003. Development and application of a cheese shred/texture Gagnaire, V., Trotel, E., le Graet, Y., Leonil, J., 2002. Role of electrostatic
map delineated by cheese rheological, sensory and chemical analysis. interactions in the curd of Emmental cheese. Int. Dairy J. 12, 601–608.
Annual Report. Wisconsin Center for Dairy Research, Madison, WI, Ganesan, B., Larsen, K., Irish, D., Brothersen, C., McMahon, D.J., 2014.
USA. Manufacture and sensory analysis of reduced and low sodium Ched-
Childs, J.L., Daubert, C.R., Stefanski, L., Foegeding, E.A., 2007. Factors dar and Mozzarella cheeses. J. Dairy Sci. 97, 1970–1982.
regulating cheese shreddability. J. Dairy Sci. 90, 2163–2174. Gascolgne, T., Jewett, B., Ochsner, P., 2002. Method of making pasta
Chow, J.J., Batt, C.A., Sinskey, A.J., 1988. Characteristics of Lactoba- filata cheese. US Patent 6,440,481.
cillus bulgaricus bacteriophage ch2. Appl. Environ. Microbiol. 54, Gaucheron, F., Le Graët, Y., Boyabal, E., Piot, M., 1997. Binding of cat-
1138–1142. ions to casein molecules: importance of physicochemical conditions.
Creamer, L.K., 1985. Water absorption by renneted casein micelles. Milchwissenschaft 52, 322–327.
Milchwissenschaft 40, 589–591. Ge, Q., Almena-Aliste, M., Kindstedt, P.S., 2002. Reversibility of pH-in-
Dahlstrom, D.G., Wiegand, J., Aimutis, W.R., 2001. Pasta filata cheese. duced changes in the calcium distribution and melting characteristics
US Patent 6,319,526. of Mozzarella cheese. Austr. J. Dairy Technol. 57, 3–9.
Dave, R.I., McMahon, D.J., Broadbent, J.R., Oberg, C.J., 2001. Revers- Gerla, P.E., Rubiolo, A.C., 2003. A model for determination of multicom-
ibility of the temperature-dependent opacity of nonfat Mozzarella ponent diffusion coefficients in foods. J. Food Eng. 56, 401–410.
cheese. J. Dairy Sci. 84, 2364–2371. Ghiglietti, R., Francolino, S., Passolungo, L., Locci, F., Mucchetti, G.,
Dave, R.I., Oberg, C.J., McMahon, D.J., 2003a. Influence of coagulant 2005. Mozzarella: standardizzare il latte con le proteine concentrate.
level on proteolysis and functionality of Mozzarella cheese made us- Latte 30, 94–99.
ing direct acidification. J. Dairy Sci. 86, 114–126. Govindasamy-Lucey, S., Jaeggi, J.J., Johnson, M.E., Wang, T., Lucey,
Dave, R.I., Sharma, P., McMahon, D.J., 2003b. Melt and rheological prop- J.A., 2005. Use of cold ultrafiltered retentates for standardization of
erties of Mozzarella cheese as affected by starter culture and coagulat- milks for pizza cheese: impact on yield and functionality. Int. Dairy
ing enzymes. Lait 83, 61–77. J. 15, 941–955.
Dimitreli, G., Thomareis, A.S., 2004. Effect of temperature and chemical Gravier, N.G., Zaritzky, N.E., Califano, A.N., 2004. Viscoelastic behavior
composition on processed cheese apparent viscosity. J. Food Eng. 64, of refrigerated and frozen low-moisture Mozzarella cheese. J. Food
265–271. Sci. 9, 123–128.
Dubuy, M.M., 1980. The French art of shredding cheese. Food Proc. Ind. Guinee, T.P., 2004. Salting and the role of salt in cheese. Int. J. Dairy
49, 52–53. Technol. 57, 99–109.
Farkye, N.Y., Kiely, L.J., Allshouse, R.D., Kindstedt, P.S., 1991. Prote- Guinee, T.P., O’Callaghan, D.J., 1997. The use of a simple empirical
olysis in Mozzarella cheese during refrigerated storage. J. Dairy Sci. method for objective quantification of the stretchability of cheese on
74, 1433–1438. cooked pizza pies. J. Food Eng. 31, 147–161.
Farrell, Jr., H.M., Pessen, H., Kumosinski, T.F., 1989. Water interactions Guinee, T.P., Feeney, E.P., Auty, M.A.E., Fox, P.F., 2002. Effect of pH
with bovine caseins by hydrogen 2 nuclear magnetic resonance relax- and calcium concentration on some textural and functional properties
ation studies: structural implications. J. Dairy Sci. 72, 562–574. of Mozzarella cheese. J. Dairy Sci. 85, 1655–1669.
Feeney, E.P., Fox, P.F., Guinee, T.P., 2001. Effect of ripening temperature Guinee, T.P., Harrington, D., Corcoran, M.O., Mulholland, E.O., Mullins,
on the quality of low moisture Mozzarella cheese. 1. Composition and C., 2000. The composition and functional properties of commercial
proteolysis. Lait 81, 463–474. Mozzarella, Cheddar, and analogue pizza cheese. Int. J. Dairy Tech-
Ferrari, E., Gamberi, M., Manzini, R., Pareschi, A., Persona, A., Regat- nol. 53, 51–56.
tieri, A., 2003. Redesign of the Mozzarella cheese production process Gunasekaran, S., Ak, M.M., 2003. Measuring cheese stretchability.
through development of a micro-forming and stretching extruder sys- Cheese Rheology and Texture. CRC Press, Boca Raton, FL, USA,
tem. J. Food Eng. 59, 13–23. pp. 377–397.
Fife, R.L., McMahon, D.J., Oberg, C.J., 1996. Functionality of low fat Guo, M.R., Kindstedt, P.S., 1995. Age related changes in the water phase
Mozzarella cheese. J. Dairy Sci. 79, 1903–1910. of Mozzarella cheese. J. Dairy Sci. 78, 2099–2107.
Henry, T., Hunt, C., Urben, J., 2006. Process for making cheese. US Pat- Kindstedt, P.S., Larose, K.L., Gilmore, J.A., Davis, L., 1996. Distribution
ent 6,998,145. of salt and moisture in Mozzarella cheese with soft surface defect. J.
Hicsasmaz, Z., Shippelt, L., Rizvi, S.S.H., 2004. Evaluation of Mozza- Dairy Sci. 79, 2278–2283.
rella cheese stretchability by the ring-and-ball method. J. Dairy Sci. Klaenhammer, T.D., 1989. Potential for the development of bacteriophage
87, 1993–1998. resistant thermophilic cultures. Proc. 26th Annual Marschall Italian
Holmes, D.G., Duersch, J.W., Ernstrom, C.A., 1977. Distribution of milk Cheese Seminar, Madison, WI, USA, pp. 57–70.
clotting enzymes between curd and whey and their survival during Kuo, M.-I., Gunasekaran, S., 2003. Effect of frozen storage on physical
cheddar cheesemaking. J. Dairy Sci. 60, 862–869. properties of pasta filata and non-pasta filata Mozzarella cheeses. J.
Hongxu, N., Guansekaran, S., 2004. Image processing algorithm for Dairy Sci. 86, 1108–1117.
cheese shred evaluation. J. Food Eng. 61, 37–45. Kuo, M.-I., Gunasekaran, S., 2009. Effect of freezing and frozen storage
Hussain, I., Yan, J., Grandison, A.S., Bell, A.E., 2012. Effects of gelation on microstructure of Mozzarella and pizza cheeses. LWT Food Sci.
temperature on Mozzarella-type curd made from buffalo and cows’ Technol. 42, 9–16.
milk: 2. Curd yield, overall quality and casein fractions. Food Chem. Kuo, M.-I., Anderson, M.E., Gunasekaran, S., 2003. Determining effects
135, 1404–1410. of freezing on pasta filata and non-pasta filata Mozzarella cheeses by
Hutkins, R., Halambeck, S.M., Morris, H.A., 1986. Use of galactose- nuclear magnetic resonance imaging. J. Dairy Sci. 86, 2525–2536.
fermenting Streptococcus thermophilus in the manufacture of Swiss, Lahbib-Mansais, Y., Mata, M., Ritzenthaler, P., 1988. Molecular taxono-
Mozzarella, and short-method Cheddar cheese. J. Dairy Sci. 69, 1–8. my of Lactobacillus phages. Biochimie 70, 429–435.
Jarvis, A.W., 1989. Bacteriophages of lactic acid bacteria. J. Dairy Sci. Licitra, G., Ogier, J.C., Parayre, S., Pediliggieri, C., Carnemolla, T.M.,
72, 3406–3428. Falentin, H., Madec, M.N., Carpino, S., Lortal, S., 2007. Variability of
Johnson, M.E., Olson, N.F., 1985. Nonenzymatic browning of Mozzarella bacterial biofilms of the “tina” wood vats used in the Ragusano chee-
cheese. J. Dairy Sci. 68, 3143–3147. semaking process. Appl. Environ. Microbiol. 73, 6980–6987.
Johnston, D.E., Darcy, P.C., 2000. The effects of high pressure treatment Liem, D.G., Miremadi, F., Keast, R.S., 2011. Reducing sodium in foods:
on immature Mozzarella cheese. Milchwissenschaft 55, 617–620. The effect on flavor. Nutrients 3, 694–711.
Joshi, N.S., Muthukumarappan, K., Dave, R.I., 2003. Understanding the Low, D., Ahlgren, J., Horne, D., McMahon, D.J., Oberg, C.J., Broadbent,
role of calcium in functionality of part skim Mozzarella cheese. J. J.R., 1998. Role of Streptococcus thermophilus MR-1C capsular exo-
Dairy Sci. 86, 1918–1926. polysaccharide in cheese moisture retention. Appl. Environ. Micro-
Joshi, N.S., Muthukumarappan, K., Dave, R.I., 2004a. Effects of reduced- biol. 64, 2147–2151.
calcium, test temperature and storage on stretchability of part-skim Lu, Y., McMahon, D.J., 2015. Effects of sodium chloride salting and
Mozzarella cheese. Austr. J. Dairy Technol. 59, 60–65. substitution with potassium chloride on whey expulsion of Cheddar
Joshi, N.S., Muthukumarappan, K., Dave, R.I., 2004b. Viscoelastic prop- cheese. J. Dairy Sci. 98, 78–88.
erties of part skim Mozzarella cheese: effect of calcium, storage, and Lucey, J.A., Johnson, M.E., Horne, D.S., 2003. Perspectives on the ba-
test temperature. Int. J. Food Prop. 7, 239–252. sis of the rheology and texture properties of cheese. J. Dairy Sci. 86,
Joshi, N.S., Muthukumarappan, K., Dave, R.I., 2004c. Modeling rheologi- 2725–2743.
cal characteristics and calcium content of Mozzarella cheese. J. Food Luo, J., Pan, T., Guo, H.Y., Ren, F.Z., 2013. Effect of calcium in brine on
Sci. 69, FEP97–FEP101. salt diffusion and water distribution of Mozzarella cheese during brin-
Joshi, N.S., Muthukumarappan, K., Dave, R.I., 2004d. Effect of calcium ing. J. Dairy Sci. 96, 824–831.
on microstructure and meltability of part skim Mozzarella cheese. J. Ma, X., James, B., Balaban, M.O., Zhan, L., Emanuelsson-Patterson,
Dairy Sci. 87, 1975–1985. E.A.C., 2013b. Quantifying blistering and browning properties of
Kennedy, S.M., 2013. Natural sliced and grated cheese sales rise. Dairy Mozzarella cheese. Part II: cheese with different salt and moisture
Foods 114 (12), 24. contents. Food Res. Int. 54, 917–921.
Kiely, L.J., Kindstedt, P.S., Hendricks, G.M., Levis, J.E., Yun, J.J., Bar- Ma, X., James, B., Zhang, L., Emanuelsson-Patterson, E.A.C., 2013a. Cor-
bano, D.M., 1993. Age related changes in the microstructure of Moz- relating Mozzarella cheese properties to its production processes and
zarella cheese. Food Struct. 12, 13–20. microstructure quantification. J. Food Eng. 115, 154–163.
Kindstedt, P.S., 1995. Factors affecting the functional characteristics of un- Ma, X., James, B., Zhang, L., Emanuelsson-Patterson, E.A.C., 2011. Cor-
melted and melted Mozzarella cheese. In: Malin, E.L., Tunick, M.H. relating Mozzarella cheese properties to production processes by rheo-
(Eds.), Chemistry of Structure-Function Relationships in Cheese. Ple- logical, mechanical and microstructure study: Meltability study and
num Press, New York, NY, USA, pp. 27–41. activation energy. Procedia Food Sci. 1, 536–544.
Kindstedt, P., Caric, M., Milanovic, S., 2004. Pasta-filata cheeses. In: Fox, Ma, X., James, B., Zhang, L., Emanuelsson-Patterson, E.A.C., 2012. The
P.F., McSweeney, P.L.H., Cogan, T.M., Guinee, T.P. (Eds.), Cheese stretchability of Mozzarella cheese evaluated by a temperature-con-
Chemistry, Physics and Microbiology, Vol. 2, Major Cheese Groups. trolled 3-prong hook test. J. Dairy Sci. 95, 5561–5568.
third ed. Elsevier Academic Press, London, UK, pp. 251–277. Malin, E.L., Brown, M.E., 1995. Influence of casein peptide conforma-
Kindstedt, P.S., Guo, M.R., Viotto, W.H. Yun, J.J., Barbano, D.M., 1995. tions on the textural properties of cheeses. In: Malin, E.L., Tunick,
Effect of screw speed and residence time at high stretching tempera- M.H. (Eds.), Chemistry of Structure-Function Relationships in
ture on composition, proteolysis, functional properties and the water Cheese. Plenum Press, New York, NY, USA, pp. 303–310.
phase of Mozzarella cheese. Proc. 32nd Annual Marschall Italian Marshall, V.M., 1987. Lactic acid bacteria: starters for flavour. FEMS Mi-
Cheese Seminar, Madison, WI, USA, pp. 56–72. crobiol. Lett. 46, 327–336.
Kindstedt, P.S., Rippe, J.K., Duthie, C.M., 1989. Measurement of Moz- Matzdorf, B., Cuppett, S.L., Keeler, L., Hutkins, R.W., 1994. Browning
zarella cheese melting properties by helical viscometry. J. Dairy Sci. of Mozzarella cheese during high temperature pizza baking. J Dairy
72, 3117–3122. Sci. 77, 2850–2853.
Mauriello, G., Moio, L., Genovese, A., Ercolini, D., 2003. Relationships Mitsoulis, W., Hatzikiriakos, S.G., 2009. Rolling of Mozzarella cheese:
between flavoring capabilities, bacterial composition, and geographi- experiments and simulations. J. Food Eng. 91, 269–279.
cal origin of natural whey cultures used for traditional water-buffalo Morales-Celaya, M.F., Lobato-Calleros, C., Alvarez-Ramirez, J., Vernon-
Mozzarella cheese manufacture. J. Dairy Sci. 86, 486–497. Carter, E.J., 2012. Effect of milk pasteurization and acidification
Mayer, M., 2011. String cheese sales increase. Dairy Foods. Available from: method on the chemical composition and microstructure of a Mexican
http://www.dairyfoods.com/articles/87900-string-cheese-sales-increase pasta filata cheese. LWT Food Sci. Technol. 45, 132–141.
McCoy, D.R., 1997. Italian type cheeses. Cultures for the Manufacture of Morea, M., Baruzzi, F., Cappa, F., Conconcelli, P.S., 1998. Molecular
Dairy Products. Chr. Hansen, Inc, Milwaukee, WI, USA, pp. 75–83. characterization of the Lactobacillus community in traditional pro-
McMahon, D.J., Motawee, M.M., McManus, W.R., 2009. Influence of cessing of Mozzarella cheese. Int. J. Food Microbiol. 43, 53–60.
brine concentration and temperature on composition, microstructure Morea, M., Baruzzi, F., Cocconcelli, P.S., 1999. Molecular and physiolog-
and yield of feta cheese. J. Dairy Sci. 92, 4169–4179. ical characterization of dominant bacterial populations in traditional
McMahon, D.J., Brown, R.J., 1984. Enzymic coagulation of casein mi- Mozzarella cheese processing. J. Appl. Microbiol. 87, 574–582.
celles: a review. J. Dairy Sci. 67, 919–929. Moyes, B., 2003. Correlation between the USU stretch test and the pizza
McMahon, D.J., Oberg, C.J., McManus, W.R., 1993. Functionality of fork test. M.Sc. Thesis, Utah State University, Logan, UT, USA.
Mozzarella cheese. Austr. J. Dairy Technol. 48, 99–104. Moynihan, A.C., Govindasamy-Lucey, S., Jaeggi, J.J., Johnson, M.E., Lu-
McMahon, D.J., Oberg, C.J., 2000. Manufacture of lower-fat and fat-free cey, J.A., McSweeney, P.L.H., 2014. Effect of camel chymosin on the
pizza cheese. U.S. Patent No. 6,113,953. texture, functionality, and sensory properties of low-moisture, part-
McMahon, D.J., Oommen, B.S., 2008. Supramolecular structure of the ca- skim Mozzarella cheese. J. Dairy Sci. 97, 85–96.
sein micelle. J Dairy Sci. 91, 1709–1721. Muliawan, E.B., Hatzikiriakos, S.G., 2008. Rheology of Mozzarella
McMahon, D.J., Alleyne, M.C., Fife, R.L., Oberg, C.J., 1996. Use of fat cheese: extrusion and rolling. Int. Dairy J. 18, 615–623.
replacers in low-fat Mozzarella cheese. J. Dairy Sci. 79, 1911–1921. Muthukumarappan, K., Wang, Y.-C., Gunasekaran, S., 1999. Estimating
McMahon, D.J., Fife, R.L., Oberg, C.J., 1999. Water partitioning in Moz- softening point of cheeses. J. Dairy Sci. 82, 2280–2286.
zarella cheese and its relationship to cheese meltability. J. Dairy Sci. Nauth, R.K., Ruffie, D., 1995. Microbiology and biochemistry of reduced-
82, 1361–1369. fat cheese. In: Malin, E.L., Tunick, M.H. (Eds.), Chemistry of Struc-
McMahon, D.J., Paulson, B.M., Oberg, C.J., 2005. Influence of calcium, ture-Function Relationships in Cheese. Plenum Press, New York, NY,
pH and moisture on protein matrix structure and functionality in direct USA, pp. 345–357.
acidified nonfat Mozzarella cheese. J. Dairy Sci. 88, 3754–3763. Nazarenko, S., Bensason, S., Hiltner, A., Baer, E., 1994. The effect of tem-
McMahon, D.J., Oberg, C.J., Drake, M.A., Farkye, N., Moyes, L.V., Ar- perature and pressure on necking of polycarbonate. Polymer (Guildf.)
nold, M.R., Ganesan, B., Steele, J., Broadbent, J.R., 2014. Impact of 35, 3883–3892.
sodium, potassium, magnesium, and calcium salt cations on pH, prote- Ni, H., Gunasekaran, S., 2004. Image processing algorithm for cheese
olysis, organic acids, and microbial populations during storage of full shred evaluation. J. Food Eng. 61, 37–45.
fat Cheddar cheese. J. Dairy Sci. 97, 4780–4798. Oberg, C.J., Wang, A., Moyes, L.V., Brown, R.J., Richardson, G.H.,
Melilli, C., Barbano, D.M., Caccamo, M., Tuminello, L., Carpino, S., Lici- 1991a. Effects of proteolytic activity of thermolactic cultures on phys-
tra, G., 2006. Interaction of brine concentration, brine temperature, ical properties of Mozzarella cheese. J Dairy Sci. 74, 389–397.
and presalting on salt penetration in Ragusano cheese. J. Dairy Sci. Oberg, C.J., Merrill, R.K., Moyes, L.V., Brown, R.J., Richardson, G.H.,
89, 1420–1438. 1991b. Effects of Lactobacillus helveticus culture on physical proper-
Merrill, R.K., Anderson, T.L., 2007. Process of making a homogeneous ties of Mozzarella cheese. J Dairy Sci. 74, 4101–4107.
cheese. US Patent 7,169,429. Oberg, C.J., Merrill, R.K., Brown, R.J., Richardson, G.H., 1992. Effects
Merrill, R.K., Oberg, C.J., McMahon, D.J., 1994. A method for manufac- of freezing, thawing, and shredding on low moisture, part-skim Moz-
turing reduced fat Mozzarella cheese. J. Dairy Sci. 77, 1783–1789. zarella cheese. J. Dairy Sci. 75, 1161–1166.
Metzger, L.E., Barbano, D.M., Rudan, M.A., Kindstedt, P.S., Guo, M.A., Oberg, C.J., McManus, W.R., McMahon, D.J., 1993. Microstructure of
2000. Whiteness change during heating and cooling of Mozzarella Mozzarella cheese during manufacture. Food Struct. 12, 251–258.
cheese. J. Dairy Sci. 83, 1–10. Oberg, C.J., Broadbent, J.R., Strickland, M., McMahon, D.J., 2002. Di-
Metzger, L.E., Barbano, D.M., Kindstedt, P.S., 2001. Effect of milk pre- versity in specificity of the extracellular proteinases in Lactobacillus
acidification on low fat Mozzarella cheese: III. post-melt chewiness helveticus and Lactobacillus delbrueckii subsp. bulgaricus. Letters
and whiteness. J. Dairy Sci. 84, 1357–1366. Appl. Microbiol. 34, 455–460.
Meza, B.E., Verdini, R.A., Rubiolo, A.C., 2011. Effect of freezing on the Ong, L., Dagastine, R.R., Kentish, S.E., Gras, S.L., 2012. The effect of pH
viscoelastic behavior during the ripening of a commercial low-fat soft at renneting on the microstructure, composition and texture of Ched-
cheese. Int. Dairy J. 21, 346–351. dar cheese. Food Res. Int. 48, 119–130.
Meza, B.E., Verdini, R.A., Rubiolo, A.C., 2012. Temperature dependency Oommen, B.S., McMahon, D.J., Oberg, C.J., Broadbent, J.R., Strickland,
of linear viscoelastic properties of a commercial low-fat soft cheese M., 2002. Proteolytic specificity of Lactobacillus delbrueckii subsp.
after frozen storage. J. Food Eng. 109, 475–481. bulgaricus influences functional properties of Mozzarella cheese. J.
Mills, S., Coffey, A., McAuliffe, O.E., Meijer, W.C., Hafkamp, B., Ross, Dairy Sci. 85, 2750–2758.
R.P., 2007. Efficient method for generation of bacteriophage insensi- Parente, E., Rota, M.A., Ricciardi, A., Clementi, F., 1997. Characteriza-
tive mutants of Streptococcus thermophilus yoghurt and Mozzarella tion of natural starter cultures used in the manufacture of pasta filata
strains. J. Microbiol. Methods 70, 159–164. cheese in Basilicata (Southern Italy). Int. Dairy J. 7, 775–783.
Mitsoulis, E., Abdali, S.S., Markatos, N.C., 1993. Flow simulation of Her- Pastorino, A.J., Dave, R.I., Oberg, C.J., McMahon, D.J., 2002. Tempera-
schel–Bulkley fluids through extrusion dies. Can. J. Chem. Eng. 71, ture effect on structure-opacity relationships of nonfat Mozzarella
147–160. cheese. J. Dairy Sci. 85, 2106–2113.
Pastorino, A.J., Hansen, C.L., McMahon, D.J., 2003b. Effect of pH on the Rudan, M.A., Barbano, D.M., 1998. A model of Mozzarella cheese melt-
chemical composition and structure function relationships of cheddar ing and browning during pizza baking. J. Dairy Sci. 81, 2312–2319.
cheese. J. Dairy Sci. 86, 2751–2760. Sanders, M.E., 1991. Genetic approaches for the improvement of strains
Pastorino, A.J., Ricks, N.P., Hansen, C.L., McMahon, D.J., 2003a. Effect for Italian cheese manufacture. J. Dairy Sci. 74, 3647–3655.
of calcium and water injection on structure-function relationships of Schmidt, D.G., 1982. Electron microscopy of milk and milk products:
cheese. J. Dairy Sci. 8, 122–131. problems and possibilities. Food Microstruct. 1, 151–165.
Paulson, B.M., McMahon, D.J., Oberg, C.J., 1998. Influence of salt on Schroeder, C.L., Bodyfelt, F.W., Wyatt, C.J., McDaniel, M.R., 1988. Re-
appearance, functionality, and protein arrangements in nonfat Moz- duction of sodium chloride in cheddar cheese: microbiological, and
zarella cheese. J. Dairy Sci. 81, 2053–2064. chemical properties. J. Dairy Sci. 71, 2010–2020.
Perry, D.B., McMahon, D.J., Oberg, C.J., 1997. Effect of exopolysaccha- Serrano, J., Velazquez, G., Lopetcharat, K., Ramırez, J.A., Torres, J.A.,
ride-producing cultures on moisture retention in low fat Mozzarella 2004. Effect of moderate pressure treatments on microstructure, tex-
cheese. J. Dairy Sci. 80, 799–805. ture, and sensory properties of stirred-curd cheddar shreds. J. Dairy
Perry, D.B., McMahon, D.J., Oberg, C.J., 1998. Manufacture of low fat Sci. 87, 3172–3182.
Mozzarella cheese using exopolysaccharide-producing cultures. J. Rehman, S.-U., Farkye, N.F., 2006. Effect of setting pH on the properties
Dairy Sci. 81, 563–566. of Mozzarella cheese made by direct acidification of whole milk stan-
Petersen, B.L., Dave, R.I., McMahon, D.J., Oberg, C.J., Broadbent, J.R., dardized with dry milk protein concentrate. Austr. J. Dairy Technol.
2000. Influence of capsular and ropy exopolysaccharide-producing 61, 8–12.
Streptococcus thermophilus on Mozzarella cheese and cheese whey. Rehman, S.-U., Farkye, N.Y., Yim, B., 2003. Use of dry milk protein con-
J. Dairy Sci. 83, 1952–1956. centrate in pizza cheese manufactured by culture or direct acidifica-
Piraino, P., Zotta, T., Ricciardi, A., McSweeney, P.L.H., Parente, E., 2008. tion. J. Dairy Sci. 86, 3841–3848.
Acid production, proteolysis, autolytic and inhibitory properties of Sheehan, J.J., Guinee, T.P., 2004. Effect of pH and calcium level on the
lactic acid bacteria isolated from pasta Filata cheeses: a multivariate biochemical, textural and functional properties of reduced-fat Moz-
screening study. Int. Dairy J. 18, 81–92. zarella cheese. Int. Dairy J. 14, 161–172.
Radke-Mitchell, L., Sandine, W.E., 1984. Associative growth and differ- Sheehan, J.J., Huppertz, T., Hayes, M.G., Kelly, A.L., Beresford, T.P.,
ential enumeration of Streptococcus thermophilus and Lactobacillus Guinee, T.P., 2005. High pressure treatment of reduced-fat Mozza-
bulgaricus. A review. J. Food Protect. 47, 245–248. rella cheese: effects on functional and rheological properties. Innov.
Rajagopal, S.N., Sandine, W.E., 1990. Associative growth and proteolysis Food Sci. Emerg. Technol. 6, 73–81.
of Streptococcus thermophilus and Lactobacillus bulgaricus in skim Stone, R., 1999. A study of the effects of proteolytic adjunct cultures on
milk. J. Dairy Sci. 73, 894–899. the physical and functional properties of low-fat Mozzarella cheese,
Rasmussen, H.L., 1980. In-plant experiences related to prevention and Masters Thesis, Utah State University, Logan, UT, USA.
control of bacteriophage. Proc. 17th Marschall Invitational Italian Thakar, H.H., Mehnert, D.W., Munz, W., Kettani, M.S., Zaikos, W.J.,
Cheese Seminar, Madison, WI, USA, pp. 2–7. Young, A., Fournier, M.R., Gurevich, M., 2002. Process for Mozza-
Ren, D., Chen, B., Chen, Y., Miao, S., Liu, J., 2013. The effects of k-casein rella cheese. US Patent 6,475,538.
polymorphism on the texture and functional properties of Mozzarella Thomas, M.A., 1969. Browning reaction in Cheddar cheese. Austr. J.
cheese. Int. Dairy J. 31, 65–69. Dairy Technol. 24, 185–189.
Renda, A., Barbano, D.M., Yun, J.J., Kindstedt, P.S., Mulvaney, S.J., Thunell, R.K., 1986. D.S.S. cultures and thermolactic media: applications
1997. Influence of screw speeds of the mixer at low temperature on in Italian cheese manufacture. Proc. 23rd Annual Marschall Italian
characteristics of Mozzarella cheese. J. Dairy Sci. 80, 1901–1907. Cheese Seminar. Madison, WI, USA, pp. 53–59.
Rhodes, K., 2000. System and method for making enhanced cheese. US Thunell, R.K., 1989. The application of defined strain technologies to Ital-
Patent 6,120,809. ian style cheese manufacture. Dairy Ind. Int. 54, 37–40.
Ribero, G.G., Rubiolo, A.C., Zorrilla, S.E., 2007a. Initial freezing point of Thunell, R.K., Sandine, W.E., 1985. Types of starter cultures. In: Gillil-
Mozzarella cheese. J. Food Eng. 81, 157–161. and, S.E. (Ed.), Bacterial Starter Cultures for Foods. CRC Press Inc,
Ribero, G.G., Rubiolo, A.C., Zorrilla, S.E., 2007b. Influence of the immer- Boca Raton, FL, USA, pp. 127–144.
sion freezing in NaCl solutions and of the frozen storage on the vis- Tunick, M.H., 2010. Activation energy measurements in rheological anal-
coelastic behavior of Mozzarella cheese. J. Food Sci. 72, E301–E307. ysis of cheese. Int. Dairy J. 20, 680–685.
Ribero, G.G., Rubiolo, A.C., Zorrilla, S.E., 2009. Microstructure of Moz- Tunick, M.H., Sheih, J.J., 1995. Rheology of reduced-fat Mozzarella. In:
zarella cheese as affected by the immersion freezing in NaCl solutions Malin, E.L., Tunick, M.H. (Eds.), Chemistry of Structure-Function Re-
and by the frozen storage. J. Food Eng. 91, 516–520. lationships in Cheese. Plenum Press, New York, NY, USA, pp. 7–19.
Richoux, R., Aubert, L., Roset, G., Briard-Bion, V., Kerjean, J.-R., Lopez, Tunick, M.H., Van Hekken, D.L., 2006. Chemistry and rheology of
C., 2008. Combined temperature–time parameters during the pressing cheese. In: Shahidi, F., Weenen, H. (Eds.), Food Lipids: Chemistry,
of curd as a tool to modulate the oiling-off of Swiss cheese. Food Res. Flavor, and Texture. American Chemical Society, Washington, DC,
Int. 41, 1058–1064. USA, pp. 133–141.
Rogers, N.R., McMahon, D.J., Daubert, C.R., Berry, T.R., Foeged- Tunick, M.H., Malin, E.L., Smith, P.W., Sheih, J.J., Sullivan, B.C., Mack-
ing, E.A., 2010. Rheological properties and microstructure of ey, K.L., Holsinger, V.H., 1993. Proteolysis and rheology of low fat
Cheddar cheese made with different fat contents. J. Dairy Sci. 93, and full fat Mozzarella cheeses prepared from homogenized milk. J.
4565–4576. Dairy Sci. 76, 3621–3628.
Rowney, M., Roupas, P., Hickey, M.W., Everett, D.W., 1999. Factors af- USDA, 1980. USDA Specifications for Mozzarella cheeses. Agricultural
fecting the functionality of Mozzarella cheese. Austr. J. Dairy Tech- Marketing Service, United States Department of Agriculture, Wash-
nol. 54, 94–102. ington, DC, USA.
USDA, 2014. Dairy products 2013 Summary. United States Department Yu, C., Gunasekaran, S., 2005b. Modeling of melt conveying and
of Agriculture, National Agricultural Statistics Service, Washington, heat transfer in a twin-screw cheese stretcher. J. Food Eng. 70,
DC, USA, p. 35. 245–252.
Van Hekken, D.L., Tunick, M.H., Malin, E.L., Holsinger, V.H., 2007. Yun, J.J., Barbano, D.M., Kindstedt, P.S., 1993. Mozzarella cheese: im-
Rheology and melt characterization of low-fat and full fat Mozzarella pact of coagulant type on chemical composition and proteolysis.
cheese made from microfluidized milk. LWT Food Sci. Technol. 40, J. Dairy Sci. 76, 3648–3656.
89–98. Yun, J.J., Barbano, D.M., Larose, K.L., Kindstedt, P.S., 1994. Effect of
van Hooydonk, A.C.M., Hagedoorn, H.G., Boerrigter, I.J., 1986. pH- mixer stretching temperature, chemical composition, microstructure,
induced physico-chemical changes of casein micelles in milk and proteolysis, and functional properties of Mozzarella cheese. J. Dairy
their effect on renneting. 1. Effect of acidification on physicochemical Sci. 77 (Suppl. 1), 34.
properties. Neth. Milk Dairy J. 40, 281–296. Yun, J.J., Barbano, D.M., Kiely, L.J., Kindstedt, P.S., 1995. Mozzarella
Verdini, R.A., Zorrilla, A.E., Rubiolo, A.C., 2005. Effects of the freez- cheese: impact of rod to coccus ratio on chemical composition, prote-
ing process on proteolysis during the ripening of Port Salut Argentino olysis, and functional properties. J. Dairy Sci. 78, 751–760.
cheeses. Int. Dairy J. 15, 363–370. Zaikos, W.J., Mehnert, D.W., Kerrigan, G.L., 1999. Process and formula-
Wadhwani, R., McManus, W.R., McMahon, D.J., 2012. Improvement in tion for improved texture and melt of reduced fat cheese product. US
melting and baking properties of low fat Mozzarella cheese. J. Dairy Patent 5,876,770.
Sci. 94, 1713–1723. Zisu, B., Shah, N.P., 2005. Low-fat Mozzarella as influenced by microbial
Wang, H.-H., Sun, D.-W., 2001. Evaluation of the functional properties exopolysaccharides, preacidification, and whey protein concentrate.
of Cheddar cheese using a computer vision method. J. Food Eng. 49, J. Dairy Sci. 88, 1973–1985.
49–53. Zisu, B., Shah, N.P., 2007. Texture characteristics and pizza bake proper-
Wang, H.-H., Sun, D.-W., 2003. Assessment of cheese browning af- ties of low-fat Mozzarella cheese as influenced by pre-acidification
fected by baking conditions using computer vision. J. Food Eng. 56, with citric acid and use of encapsulated and ropy exopolysaccharide
339–345. producing cultures. Int. Dairy J. 17, 985–997.
Whitehead, W.E., Matalon, M.E., Ayres, J.W., Sandine, W.E., 1991. Zorrilla, S.E., Rubiolo, A.C., 2005a. Mathematical modeling for immer-
Evaluating performance of thermophilic coccus-rod cultures. Proc. sion chilling and freezing of foods. Part I: model development. J. Food
28th Annual Marschall Italian Cheese Seminar. Madison, WI, USA, Eng. 66, 329–338.
pp. 11–30. Zorrilla, S.E., Rubiolo, A.C., 2005b. Mathematical modeling for immer-
Yu, C., Gunasekaran, S., 2005a. A systems analysis of pasta filata process sion chilling and freezing of foods. Part II: model solution. J. Food
during Mozzarella cheesemaking. J. Food Eng. 69, 399–408. Eng. 66, 339–351.

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Chapter 40

INTRODUCTION baking on pizza, in which it is specifically manufactured

To manufacture cheese with 30%–45% fat-in-dry-matter

FIGURE 40.6 Low-moisture Mozzarella cheese curd being fed into

FIGURE 40.5 Milling of low-moisture Mozzarella cheese (LMMC)

of LMMC after cooling and brining, Ferrari et al. (2003)

STEPS IN CHEESE MANUFACTURE

FIGURE 40.11 Molding machine for making blocks of LMMC.

FIGURE 40.20 Scanning electron micrograph of low-moisture part-

starter culture (Klaenhammer, 1989). As a consequence, CHEESE CHEMISTRY

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