Bioactive Peptides

BACKGROUND: Bean seeds are an inexpensive source of protein. Anthracnose disease caused by the fungus Colletotrichum lindemuthianum results in serious losses in common bean (Phaseolus vulgaris L.) crops worldwide, affecting any above-ground plant part, and protein dysfunction, inducing the synthesis of proteins that allow plants to improve their stress tolerance. The aim of this study was to evaluate the use of beans damaged by anthracnose disease as a source of peptides with angiotensin-converting enzyme (ACE-I)-inhibitory activity. RESULTS: Protein concentrates from beans spoiled by anthracnose disease and from regular beans as controls were prepared by alkaline extraction and precipitation at isolelectric pH and hydrolysed using Alcalase 2.4 L. The hydrolysates from spoiled beans had ACE-I-inhibitory activity (IC50 0.0191 mg protein mL-1) and were very similar to those from control beans in terms of ACE-I inhibition, peptide electrophoretic profile and kinetics of hydrolysis. Thus preparation of hydrolysates using beans affected by anthracnose disease would allow for revalorisation of this otherwise wasted product. CONCLUSION: The present results suggest the use of spoiled bean seeds, e.g. anthracnose-damaged beans, as an alternative for the isolation of ACE-I-inhibitory peptides to be further introduced as active ingredients in functional foods. © 2012 Society of Chemical Industry.

The present investigation was carried out to determine the possible bioactive components of tuber of Ruellia tuberosa L. (Acanthaceae) using GC-MS analysis. Twenty five compounds were identified. The prevailing compounds in the ethanol extract of tuber of R. tuberosa were Lupeol (68.14%), Stigmasterol (8.89%), á-Sitosterol (3.99%), Sucrose (2.24%), Cholest-5-ene, 3-bromo-, (3á- (2.24%), Octadecane, 2-methyl- (2.10%), Nonadecane, 2-methyl- (1.93%), Eicosane, 2-methyl- (1.79%) Heptacosane (1.43%) and Heptacosane (1.29%).

A b s t r a c t A r t i c l e I n f o This review is a comprehensive survey of unique, unusual, and rare fatty acids incorporated into natural marine and terrestrial peptides obtained from fungi, fungal endophytes, lichenized ascomycetes, basidiomycetes, and actinomycetes. Lots of fungal peptides display important biological activities of interest, which includes antitumor, antibacterial, antimicrobial, antifungal, phototoxic, HIV inhibitory, immunosuppressive properties, and other pharmacological activities. There is no doubt that they are of great importance, especially in medicinal chemistry and/or pharmaceutical application. This review presents structures of more than 150 fatty acids, incorporated into marine and terrestrial fungal lipopeptides.

The world is aging rapidly; thus, the management of elderly health at an advanced age poses a new research challenge. The elderly is vulnerable to not only malnutrition but also hypofunction of all organs and a variety of chronic diseases such as sarcopenia, osteoporosis, gastrointestinal dysfunction, and mental problems. As the major macronutrient, food protein plays an important role in elderly health and well-being. In this chapter, the function of protein and peptide in elderly health as well as their effects on preventing aging-related disease is reviewed.

The unique composition of milk makes this basic foodstuff into an exceptional raw material for the production of new ingredients with desired properties and diverse applications in the food industry. The fractionation of milk is the key in the development of those ingredients and products; hence continuous research and development on this field, especially various levels of fractionation and separation by filtration, have been carried out. This review focuses on the production of milk fractions as well as their particular properties, applications and processes that increase their exploitation. Whey proteins and caseins from the protein fraction are excellent emulsifiers and protein supplements. Besides, they can be chemically or enzymatically modified to obtain bioactive peptides with numerous functional and nutritional properties. In this context, valorization techniques of cheese-whey proteins, by-product of dairy industry that constitutes both economic and environmental problems, are being developed. Phospholipids from the milk fat fraction are powerful emulsifiers and also have exclusive nutraceutical properties. In addition, enzyme modification of milk phospholipids makes it possible to tailor emulsifiers with particular properties. However, several aspects remain to be overcome; those refer to a deeper understanding of the healthy, functional and nutritional properties of these new ingredients that might be barriers for its use and acceptability. Additionally, in this review, alternative applications of milk constituents in the non-food area such as in the manufacture of plastic materials and textile fibers are also introduced. The unmet needs, the cross-fertilization in between various protein domains,the carbon footprint requirements, the environmental necessities, the health and wellness new demand, etc., are dominant factors in the search for innovation approaches; these factors are also outlining the further innovation potential deriving from those “apparent” constrains obliging science and technology to take them into account.

Proteomic and peptidomic studies are emerging as an important part of the holistic approach to food science and technology and have been recently applied in the study and production of bioactive peptides. Food-derived bioac-tive peptides are short amino acid chains with a known sequence that may have one or more biological activities. The proteomic and peptidomic approach to bioactive peptide studies includes bioinformatics, chemometric tools and proteomic/peptidomic methods. A proteomic and peptidomic approach applied to the study of bioactive peptides allows optimizing their production and finding peptides of interest and contributes to understand the interaction mechanisms between receptor and bioactive peptides. The objective of this review was to describe recent analytical tools used for studying various aspects of food-derived biopeptides, emphasizing their production at laboratory and industrial scale.

A B S T R A C T The present study has aimed to evaluate the microencapsulation process of the different casein hydrolysates and to assess the physical properties (moisture content, water activity, bulk density, tapped density, solubility and hygroscopicity), antioxidant activities, chemical structure (FTIR), microstructure and bitterness-masking of the spray-dried powders. The microencapsulation process was done using a laboratory spray-dryer and maltodextrin (DE = 18) as the carrier agent. The obtained results indicated the hygroscopicity of the casein hydrolysates was significantly reduced after microencapsulation process (P < 0.05). By evaluating the antioxidant properties, it became clear that the DPPH free radical scavenging activity, ABTS radical scavenging activity, hydroxyl radical scavenging activity, reducing power, Fe 2+ and Cu 2+ chelating activity were maintained as 90.4–98.5%, 77.5–91.6%, 77.2–93.1%, 95.2–99.6%, and 76.7–98.4% after the spray-drying process, respectively. FTIR spectrometry proved the presence of the hydrolysates in the structure of the microcapsules. The scanning electron microscopy images showed the production of hollow particles with a matrix-type structure. In addition, sensory evaluation of the pastilles fortified with microencapsulated and free hydrolysates suggested that the spray-drying has been effective in reducing the bitterness of these compounds.

Bioactive peptides are found in hidden or inactive sequence of amino acids in milk protein and
digestion or enzyme-mediated proteolysis while open interests advanced food processing. Biologically active
peptides, to this day have been demonstrated to be effective as the immune system stimulants, mineral
binders, opioids, antihypertensives, antithrombotic, antimicrobial, anticancer, antioxidant, increase the
absorption of calcium and lovering blood cholesterol level. The importance of bioactive peptides is associated
with effects on human health and the production of new functional foods. Therefore, today attracted the attention of many areas including life sciences, food science and nutrition and health have become supportive
of functional foods or used in pharmaceutical preparations. Besides the known biological effects in vivo
studies, but need to understand more fully the effects of some other, the results obtained from studies
conducted to date have been promising.

The economic evaluation for the production of fruit juice from the Africa star apple otherwise known as 'Agbalumo' in the south western part of Nigeria was evaluated using the NPV (Net Present value) and IRR (Internal Rate of Return) methods assuming a uniform cash flow over a 10-year plant life. Sensitivity analysis was conducted by varying the number of production days (330, 300 and 250 days) at 100% plant capacity and varying the plant capacity (100, 85 and 70%) for a 330-day production schedule. Some components of the operating cost reduced with number of days and plant capacities. The production cost and product cost per unit increased with either plant capacity utilization or the number of days. It was observed that product cost/ 500ml Tetra Pak of Agbalumo juice at 85% and 70% stood at ₦37.48 while payback time/profitability percent had better index at 300 and 250 days compared to 330 days of plant operation. The results further indicated that the plant should not be operated for less than 250 days and plant capacity utilization of 70% in the year. Flexibility in the plant capacity utilization in the range of 70%-85% for 330 days shows a good economic performance as well as result of the NPV and IRR for this operating condition.

In the present study, the alcalase-generated proteolysates obtained after 8 h of proteolysis of stone fish flesh showed the most potent antioxidant activity in terms of DPPH• radical scavenging activity (77.43%, IC50 of 0.5 mg/mL), ABTS• radical scavenging activity (92.73%, IC50 of 0.33 mg/mL) and FRAP value (39.2 mmol/100 mL FeSO4). These proteolysates profiled and characterized as antioxidative peptides. The proteolysates were initially subjected to ultrafiltration using MWCO Spin-X UF. Potent fractions were further characterized based on hydrophobicity using reversed-phase high-performance liquid chromatography (RP-HPLC) and isoelectric point using an OFFGEL isoelectric focusing fractionator. Results indicated that most of the antioxidative peptides found in fractions with a molecular weight (MW) of less than 2 kDa, hydrophilic (hydrophilicity >80%) and basic (pI = 9.7). The final purified fraction with the highest antioxidant activity was selected for peptide identification and sequencing using Q-TOF mass spectrometry. A total of four peptides were identified, from which Peptide 1 (GVSGLHID) showed the highest antioxidant activity and this has potential as a novel bioingredient of nutraceuticals and functional foods to promote human health.

Temporin-1Tl (TL) is a 13-residue frog antimicrobial peptide (AMP) exhibiting potent antimicrobial and anti-inflammatory activity. To develop novel AMP with improved anti-inflammatory activity and antimicrobial selectivity, we designed and synthesized a series of TL analogs by substituting Trp, Arg and Lys at selected positions. Except for Escherichia coli and Staphylococcus epidermidis, all TL analogs exhibited retained or increased antimicrobial activity against seven bacterial strains including three methicillin-resistant Staphylococcus aureus strains compared with TL. TL-1 and TL-4 showed a little increase in antimicrobial selectivity, while TL-2 and TL-3 displayed slightly decreased antimicrobial selectivity because of their about twofold increased hemolytic activity. All TL analogs demonstrated greatly increased anti-inflammatory activity, evident by their higher inhibition of the production tumor necrosis factor-α (TNF-α) and nitric oxide and the mRNA expression of inducible nitric oxide synthase and TNF-α in lipopolysaccharide (LPS)-stimulated RAW264.7 macrophage cells, compared with TL. Taken together, the peptide anti-inflammatory activity is as follows: TL-2 ≈ TL-3 ≈ TL-4 > TL-1 > TL. In addition, LPS binding ability of the peptides corresponded with their anti-inflammatory activity. These results apparently suggest that the anti-inflammatory activity of TL analogs is associated with the direct binding ability between these peptides and LPS. Collectively, our designed TL analogs possess improved anti-inflammatory activity and retain antimicrobial activity without a significant increase in hemolysis. Therefore, it is evident that our TL analogs constitute promising candidates for the development of peptide therapeutics for gram-negative bacterial infection.

Bioactive food ingredients are non-essential substances found in foods that can modulate one or more metabolic processes, resulting in enhanced health. Functional diets have attracted more critical than ever as an alternative to conventional treatments of many diseases. The medicinal potential of functional foods and nutraceuticals is due to some unique functional groups produced due to food metabolism and their molecular variants. Phytochemicals are biologically active, naturally occurring chemical compounds in plants with various biological properties and therapeutic benefits. While functional foods and natural bioactive compounds have been used as conventional medicines to treat chronic diseases for decades, recent scientific findings identify functional foods' health advantages and present their behavior's basic mechanisms. Phytochemicals have essential bioactive roles in the prevention and treatment of oxidative and inflammatory diseases. Plant-derived bioactive compounds can help suppress inflammation by inhibiting oxidative damage and communicating with the immune system. Many bioactive components are capable of binding to intestinal tract toxins or carcinogens. These bioactive peptides control Diet-related medical conditions such as obesity, cardiovascular diseases, and other metabolic diseases. Various bioactive compounds in common food and their therapeutic role is discussed in this review.

Keywords: Functional food, phytochemicals, bioactive peptides, therapeutic effects.

The current study was carried out for testing the inhibitory spectrum of the metabolic extract of Saccharomyces boulardii yeast against (26) bacterial isolates. The metabolic extract of Saccharomyces boulardii yeast was obtained after growth in YEPG medium and centrifuged. The broad inhibitory spectrum of yeast extract against Gram-positive bacteria and Gram-negative bacteria assay by liquid medium method and solid medium method. The highest inhibition of Enterobacter spp. and B. cereus in the solid medium were (37) mm and (35) mm respectively when adding the inhibitory substances at (100 μL) concentration while the inhibition ratio percentage in the liquid medium was (74.2%) and (72.1%) respectively for both bacteria. Less inhibition diameter for bacteria was E. coli 6 which reaches (18) mm. after adding (100μl) concentrations, while the percentage of inhibition in the liquid medium was (26.7%).

Peptides obtained from three varieties of common beans (Phaseolus vulgaris L.) named plus black (PB), azufrado higuera (AH) and pinto Saltillo (PS) presented antimicrobial, antioxidant and antihypertensive activities. Peptides were obtained from these common beans protein concentrates after treatment with Alcalase® followed by ultrafiltration using 1-, 3- and 10-kDa molecular weight cutoff membranes. Antioxidant activity was determined by the 2,2′-azino-bis (3-etilbenzotiazolin-6-sulfonic) acid method and was expressed as Trolox equivalent antioxidant capacity (TEAC). The highest antioxidant activity (630, 550 and 517 mM TEAC/mg protein) was observed in the group of peptides with a molecular weight lower than 1 kDa (F < 1) from PB, AH and PS bean varieties, respectively. Antibacterial activity was determined as susceptibility test in which ten of twelve bacteria strains showed growth inhibition with the total hydrolysates (TH) and the peptidic fraction 3–10 kDa; subsequently, the minimum inhibitory concentration was determined with the standard microdilution assay in a 96-well plates in which the peptidic fraction F < 1 kDa presented antimicrobial activity against Shigella dysenteriae with the three beans varieties at 0.1, 0.4 and 0.3 mg/mL (for PB, AH and PS, respectively). Additionally to the antimicrobial and antioxidant activities, the TH of the PB and AH bean varieties presented high inhibition of the angiotensin-I-converting enzyme (ACE-I) (IC50 = 4.34 ± 0.29 and 4.82 ± 1.59 μg/mL, respectively). And, when the peptidic fraction F3–10 kDa was tested, the AH variety showed a significant increase in the ACE-I capacity (IC50 = 1.09 ± 0.04 μg/mL). Importantly, this peptidic fraction decreased the systolic blood pressure in a spontaneously hypertensive rat model after 2 h of administration by a single interperitoneally dose.

Aim: Sheep milk-born bioactive peptides have been found to exhibit various physiological activities. The present work was designed with the aim to evaluate the effect of boiling on antidiabetic property of peptides derived from sheep milk caseinate on hydrolysis with three different proteases. Materials and Methods: In this investigation, casein prepared from raw and boiled sheep milk was hydrolyzed by three commercially available proteases (trypsin, pepsin, and chymotrypsin). These hydrolysates collected at different hydrolysis times (60, 120, 160, and 240 min) were assayed for their antidiabetic activity. Results: Among the three different enzyme hydrolysates, casein treated with chymotrypsin shows the highest antidiabetic activity among other enzymes. While the antidiabetic effect of raw milk-derived casein hydrolysates always exceeds than effect shown by boiled milk casein hydrolysates. Conclusion: The result obtained hence shows that the effect of boiling on the properties of bioactive peptides released during different enzyme digestion depends largely on the enzymatic formulation used and treatment conditions. Chymotrypsin treatment of raw casein yields peptides with maximum antidiabetic activity as compared to pepsin and trypsin. Moreover, the peptides produced after enzymatic treatment of boiled casein show reduced antidiabetic properties. Therefore, enzymatically treated raw milk casein hydrolysates may be used as effective nutritional supplements for diabetic patients, as it causes a significant inhibition of α-amylase activity.

Целью настоящей работы была оценка изменений зрительных функций у пациентов с возрастной макулярной дегенерацией (ВМД) и миопией средней и высокой степени на фоне лечения пептидным биорегулятором и поливитаминным комплексом. Материал и методы. Обследовано 60 пациентов (120 глаз) в возрасте
от 44 до 79 лет с возрастными изменениями сетчатки, разделенных на две группы в зависимости от вида лечения:
1-я группа — пациенты, получающие пептидный биорегулятор и поливитаминный комплекс; 2-я группа — пациенты, получающие только поливитаминный комплекс, а также на подгруппы в зависимости от длины ПЗО
(1-я подгруппа — с ПЗО < 26,5 мм; 2-я подгруппа — с ПЗО  26,5 мм). Оценивали изменения зрительных функций
на фоне лечения пептидным биорегулятором и поливитаминным комплексом. Результаты. Положительный ответ на предложенную терапию (повышение остроты зрения и улучшение периметрических показателей) зафиксирован у пациентов обеих групп с ПЗО < 26,5 мм, что можно объяснить исходно лучшим состоянием сетчатки.
У пациентов в подгруппе с ПЗО  26,5 мм отмечалось статистически достоверное улучшение остроты зрения
без коррекции, однако максимальная корригированная острота зрения осталась практически без изменений.
Заключение. Предложенная схема лечения может быть использована у пациентов с патологией сетчатки при
ВМД и миопии

Conversion of amyloid fibrils by many peptides/proteins involves cytotoxic helix-rich oligomers.
However, their toxicity and biophysical studies remain largely unknown due to their
highly dynamic nature. To address this, we chose two helical peptides (melittin, Mel and
pancreatic polypeptide, PP) and studied their aggregation and toxicity. Mel converted its
random coil structure to oligomeric helical structure upon binding to heparin; however, PP
remained as helix after oligomerization. Interestingly, similar to Parkinson’s associated α-
synuclein (AS) oligomers, Mel and PP also showed tinctorial properties, higher hydrophobic
surface exposure, cellular toxicity and membrane pore formation after oligomerization in the
presence of heparin. We suggest that helix-rich oligomers with exposed hydrophobic surface
are highly cytotoxic to cells irrespective of their disease association. Moreover as Mel
and PP (in the presence of heparin) instantly self-assemble into stable helix-rich amyloidogenic
oligomers; they could be represented as models for understanding the biophysical
and cytotoxic properties of helix-rich intermediates in detail.

Trp residue is considered as one of the important constituents in antimicrobial peptides (AMPs) as it presence
secured good activities in many cases. However, it is preferable to be changed because of their sensitivity
towards light. We have synthesized the short Trp-rich AMP Pac-525 and its analogues to investigate the
possibility of His(chx) as possible replacement analogue for Trp in AMPs. Based on the assay result of the
antibacterial activity including anti-MRSA activity, His(chx) is considered as good candidate for the Trp
replacement. Through these study, we found that His(chx) had several merits to design therapeutic
antimicrobial agents compare to Trp in terms of i) increasing antibacterial activity without hemolytic activity,
ii) successful in designing the short peptide (only four residues), iii) having anti-MRSA activity, iv)
overcoming the light sensitivity. Furthermore, transmission electron microscopy (TEM) and dye leakage
experiments suggested that P11 and P16 containing His(chx) kill bacteria via forming pore/ion channels on
bacterial cell membranes.

This study was aimed to generate a valuable protein hydrolysate and bioactive peptides with strong ACE-inhibitory activity in vitro and in vivo from palm kernel cake (PKC) protein. PKC protein was independently hydrolyzed by seven different proteases to produce PKC protein hydrolysates. Among those investigated, papain-produced hydrolysate revealed the highest ACE-inhibitory activity (70.9%). When normotensive rats induced with hypertension were fed the hydrolysate at a dose of 75 mg/kg body weight, their blood pressures stabilized considerably. Fractionation of the protein hydrolysate using RP-HPLC revealed a direct relationship between hydrophobicity and ACE-inhibitory activity. The fractions with relatively higher ACE-inhibitory activity were further fractionated by isoelectric focusing, out of which fractions having neutral and basic charges showing higher ACE-inhibitory activities (77% and 75%, respectively). Nine peptide sequences were identified by Q-TOF mass spectrometry, and their respective ACE-inhibitory activities evaluated. The peptide sequences YLLLK, YGIKVGYAIP, and LPWRPATNVF showed ACE-inhibitory activities of 100%; however, the best IC50 values were observed for YGIKVGYAIP, GIFE and LPWRPATNVF at 1 μM, 3 μM and 20 μM, respectively

Whey is a protein complex derived from milk, exhibit highest protein quality rating among other proteins, being touted as a functional food with number of health benefits. In the present investigation, whey proteins hydrolysates produced using trypsin enzyme to augment antioxidant activity and to assess angiotensin converting enzyme (ACE) inhibition activity. Hydrolysis parameters were standardized applying response surface methodology. The response antioxidant activity in terms of Trolox equivalent antioxidant capacity (TEAC) values was determined by radical scavenging assay method. Optimum conditions for maximum antioxidant activity were standardized at 88 °C of preheating, 7.3 pH, 0.05 enzymes to substrate ratio and hydrolysis was carried up to 8 h at 36.5 °C. Resulting peptide fractions obtained at 11.8 % of degree of hydrolysis displayed antioxidant capacity with TEAC values of 1.37 ± 0.12. The designed model found to be significant with R2 value of 0.9972 for antioxidant activ...

Mimosine is a non-protein aminoacid with various properties, such as antibacterial, anti-inflammatory, anti-cancer and anti-virus among others. Due to its structure similarity with deferiprone (DFP), mimosine is a potential excellent metal chelator. In the present work, we combine experimental and theoretical (DFT) approaches in order to investigate the properties of mimosine peptides. Six different peptides were synthesized and their complex stoichiometry and stability were characterized by means of UV-Vis spectrophotometry. Then, the binding mode and self-assembly features of the peptides were evaluated using a DFT approach, taking into account different number of mimosine amino acids and varying the length of the spacer between the mimosine residues, finding a good agreement between experimental data and computational calculations. Further elucidations of the structural properties of these peptides allowed us to propose improvements in the structure of the mimosine moiety that can lead to enhanced affinity for high-valent metals. Moreover, we demonstrate that these peptides show an anti-microbial activity against gram positive bacteria that is enhanced by the formation of a complex with iron(III) ions. The mimosine peptides could be an alternative to Antimicrobial peptides (AMPs), which are expensive and susceptible to proteolytic degradation. In summary, in the present work, we propose a new generation of multipurpose mimosine-based peptides as a new metal self-assembly chelators that could be a corner point in biomedical and nanotechnological applications.

dairy model protein) and Maltodextrin was assessed on spray drying process of honey. The obtained results revealed that no powder will be produced in drying process of honey without using supplements, while using protein in spray drying process (as low as 10%), will increase the efficiency up to 50%. Comparing to that, reaching a similar efficiency will need large amount of Maltodextrin (up to 100% w/w based on dry weight of honey). The mechanism of action of proteins has been proven by other scientists using physical property tests, powder production efficiency and glass transition temperature (Tg). Recent study showed that preferential migration of protein to the surface of droplets/particles, which reduces adhesive behavior (stickiness) between particles and dryer wall by the increase in the surface protein coverage of the particles. The mechanism of Maltodextrin to decrease the stickiness is due to the increase in the overall Tg of the honey powders.

Actinopyga lecanora, commonly known as sea cucumber, is a rich protein source. This marine protein source was hydrolyzed using six proteases to generate anti-inflammatory hydrolysates and bioactive peptides. Bromelain hydrolysates after 1 h hydrolysis exhibited the highest nitric oxide (NO) inhibitory activity reflecting anti-inflammatory activity. A sequence of two fractionation methods was employed to fractionate the peptides based on their hydrophobicity using a semi-preparative RP-HPLC and isoelectric points using isoelectric focusing technique. Based on these fractionation methods, basic peptides with relatively higher hydrophobicity provided higher NO-inhibitory activity than did acidic peptides. Furthermore, using Q-TOF mass spectrometry; 12 peptide sequences were successfully identified. The inhibitory effect of the purified peptides from A. lecanora on NO production by lipopolysaccharide (LPS)-stimulated RAW 264.7 cells was investigated. The three identified bioactive peptides, namely LREMLSTMCTARGA, AVGPAGPRG and VAPAWGPWPKG, exhibited the highest NO-inhibitory activity with values of 76.3, 66.6 and 69.9%, respectively. These results revealed that A. lecanora could be used as an economical protein source for the production of high-value bioactive peptides with potent anti-inflammatory activity using RAW 264.7 cell lines as model. These peptides may be useful ingredients in food and pharmaceutical applications.

Cancer has become a serious concern in public health. Harmful side effects and multidrug resistance of traditional chemotherapy have prompted urgent needs for novel anticancer drugs or therapeutic approaches. Anticancer peptides (ACPs) have become promising molecules for novel anticancer agents because of their unique mechanism and several extraordinary properties. Most α-helical ACPs target the cell membrane, and interactions between ACPs and cell membrane components are believed to be the key factor in the selective killing of cancer cells. In this review, we focus on the exploitation of the structure and function of α-helical ACPs, including the distinction between cancer and normal cells, the proposed anticancer mechanisms, and the influence of physicochemical parameters of α-helical ACPs on the biological activities and selectivity against cancer cells. In addition, the design and modification methods to optimize the cell selectivity of α-helical ACPs are considered. Furthermore, the suitability of ACPs as cancer therapeutics is discussed.

In this study, a potent angiotensin-converting enzyme
(ACE)-inhibitory activity was found in a commercial
kefir made from caprine milk. The low molecular
mass peptides released from caseins during fermentation
were mainly responsible for this activity. Sixteen
peptides were identified by HPLC-tandem mass spectrometry.
Two of these peptides, with sequences
PYVRYL and LVYPFTGPIPN, showed potent ACE-inhibitory
properties. The impact of gastrointestinal digestion
on ACE-inhibitory activity of kefir peptides was
also evaluated. Some of these peptides were resistant
to the incubation with pepsin followed by hydrolysis
with Corolase PP. The ACE-inhibitory activity after
simulated digestion was similar to or slightly lower
than unhydrolyzed peptides, except for peptide β-casein
f(47-52) (DKIHPF), which exhibited an activity 8 times
greater after hydrolysis.

A staggering 1.3 billion ton of edible foods are wasted globally per year, primarily due to loss of texture and moisture during storage. Current emulsifiers/humectants like PEG and sorbitol used to stabilize food texture and composition are known to display toxic effects at higher doses. This has lead to a search for naturally available and non toxic alternatives. Since hydrolysates of the extra cellular protein collagen are known to display several physiological activities, this study was conducted to evaluate the potential of collagen hydrolysates (CH) used as emulsifiers/humectants in food. Collagen was isolated from the skin and swim bladder of Catla catla and was identified to be collagen type I based on its electrophoretic and elution profile which displayed double peaks at 100 kDa. Bacterial collagenase was used for hydrolysing and fragmentation was confirmed by altered electrophoretic and elution profile displaying mass of 7-12kD. CH exhibited an emulsification activity of 2.5±0.78 m 2 /g at 0.005% concentration and emulsion stability of 33±1.2 minutes, significantly similar [p<0.05] to the positive control. The CH sample could successfully retain 97±0.25 % of added water during a period of seven days. The CH sample displayed a mere 2+1.04% haemolytic activity and was confirmed non-toxic. CH can revolutionize the current food and health industry as they display high bioavailability and bio compatibility with no side effects, and can be isolated in bulk from marine industry processing waste.

Winged bean [Psophocarpus tetragonolobus (L.) DC.] seed is a potential underexploited source of vegetable protein due to its high protein content. In the present work, undefatted and defatted winged bean seed hydrolysates, designated as UWBSH and DWBSH, respectively were produced separately by four proteolytic enzymes namely Flavourzyme, Alcalase, Bromelain, and Papain using pH-stat method in a batch reactor. Enzymatic hydrolysis was carried out over a period of 0.5 to 5 h. UWBSH and DWBSH produced were tested for their ACE inhibitory activity in relation to the hydrolysis time and degree of hydrolysis (DH). Maximum ACE inhibitory activity, both for UWBSH and DWBSH, were observed during 3 to 5 h of hydrolysis. Both, UWBSH (DH 91.84 %), and DWSBH (DH 18.72 %), produced by Papain at 5 h hydrolysis, exhibited exceptionally high ACE inhibitory activity with IC 50 value 0.064 and 0.249 mgmL −1 , respectively. Besides, papain-produced UWBSH and DWBSH were further frac-tionated into three fractions based on molecular weight (UWBSH-I, <10 kDa; UWBSH-II, <5 kDa; UWBSH-III, <2 kDa) and (DWBSH-I, <10 kDa; DWBSH-II, <5 kDa; DWBSH-III, <2 kDa). UWBSH-III revealed the highest ACE inhibitory activity (IC 50 0.003 mgmL −1) compared with DWBSH-III (IC 50 0.130 mgmL −1). The results of the present investigation revealed that winged bean seed hydro-lysates can be explored as a potential source of ACE inhibitory peptides suggesting their uses for physiological benefits as well as for other functional food applications. Keywords Undefatted and defatted winged bean seed. Proximate analysis. ACE inhibitory activity. IC 50 value. Degree of hydrolysis. pH-stat titration

Abstract-l. Carotid blood pressure from anesthetized B. jururaca snakes was recorded in order to study
angiotensin action in this reptile.
2. Whereas [Asn1,Val5] AII and AIII were less potent than [Asp1,Ile5] AII and [Asp1,Val5] AII, [Sar1, Ile5]
AII was slightly more potent.
3. Captopril abolished the responses to AI (0.01-3 pg/kg).
4. [Sar1,Ala8] AII was uneffective but [Sar1,Leu8] AII or phenoxybenzamine were able to reduce AII
vasopressor responses.
5. These results led to the conclusion that the vasopressor response of AII in B. jararaca is due to an
interaction with its own receptor but, part of the AII receptor population seems to be coupled to the
sympatho-adrenal system. Moreover, structural requirements seem to be necessary for the AII response in B. jararaca