No. 12, Myllappanahalli, Yelahanka, Bengaluru North-560089.

(Affiliated to CBSE Code: 830332)

CBSE CLASS – 12

CHEMISTRY
INVESTIGATORY PROJECT
(2023-2024)
TOPIC : To study digestion of starch by salivary amylase and effect of pH
and temperature on it.

SUBMITTED TO : Ms Princy
SUBMITTED BY : Ms Leena M
CLASS SECTION : XII Science
REG. NUMBER :
1
 CERTIFICATE
This is to certify that Leena M of class 12 has satisfactorily completed
his/her Project Report in__________________on the topic _______________
_______________________________________ as prescribed by the Central
Board of Secondary Education for the partial fulfilment of AISSCE 2023– 24.

Date :

Signatures:
Internal Examiner : External Examiner :

Principal : School Seal :

Name of the candidate :

Registration No. :
Examination centre :
Date of Practical Examination :

2
 ACKNOWLEDGEMENT

In the accomplishment of this project successfully, my family

members have best owned upon me their blessings and the heart
pledged support. I am utilizing this opportunity to thank all who have
been concerned with this project.

Primarily I would thank god for being able to complete this project
with success. Then I would like to thank my principal Mrs. Rani
Sebastian and Biology teacher Mrs. Mamatha Balachandra whose
valuable guidance has been the ones that helped me patch this project
and make it full proof success. Her suggestions and instructions have
served as the major contributor towards the completion of the project.
At the same time I can’t forget to express my thankfulness to Mrs
Asha for constant support.

Then I would like to thank my parents who have helped me with

their valuable suggestions and guidance has been very helpful in
various phases of the completion of the project. Last but not the least I
would like to thank my classmates who have helped me a lot.

3
 INDEX

Sl.no Topic Pg.no

1 Certificate 2

2 Acknowledgement 3

3 Introduction 5-14

4 Experiment 15-16

5 Observation 15

7 Conclusion 17

8 Evidence 18

9 Bibliography 19

4
 OBJECTIVE:

“To Study the digestion of starch by salivary amylase and effect of

temperature and pH on it”
And:
 To study digestion of starch by saliva.
 To study the effect of temperature on the digestion of starch by saliva.
 To study the effect of pH on the salivary digestion of starch.

INTRODUCTION:

Every health book insists on the chewing of food. The act of chewing
stimulates the excretion of saliva. Saliva mixes up with the food and helps its
digestion. That is, the enzyme ptyalin or amylase present in human saliva
hydrolyse the big molecules of food into many molecules. For example starch
into mono-saccharides maltose and glucose; proteins into amino acids and fats

5
into fatty acids and glycerol. Thus saliva not only helps in digestion of food but
convert it into energy generating substances. Further, enzymes and their
activity are very sensitive to temperature and pH. Even a slight variation in
these two factors, can disrupt the action of enzymes. In other words, digestion
of food by salivary amylase is also effected by pH and temperature and can be
verified experimentally. For example, hydrolysis of starch can be verified by
testing it with iodine solution. Starch forms blue coloured complex with iodine.
If no starch is present in a system it will not give blue colour with iodine.
Salivary amylase is a glucose-polymer cleavage enzyme that is produced by the
salivary glands. It comprises a small portion of the total amylase excreted,
which is mostly made by the pancreas. Amylases digest starch into smaller
molecules, ultimately yielding maltose, which in turn is cleaved into two
glucose molecules by maltase. Starch comprises a significant portion of the
typical human diet for most nationalities. Given that salivary amylase is such a
small portion of total amylase, it is unclear why it exists and whether it conveys
an evolutionary advantage when ingesting starch. This review will consider the
impact of salivary amylase on oral perception, nutrient signalling, anticipatory
metabolic reflexes, blood sugar, and its clinical implications for preventing
metabolic syndrome and obesity.
Saliva has many crucial roles in promoting health, including protecting the oral
cavity and facilitating eating. Within the mouth, saliva hydrates mucosal
tissues, removes cell and food debris, buffers oral pH, lubricates the oral cavity
aiding mastication and preventing dental wear, forms food bole to assist
swallowing, protects against teeth demineralization, has antimicrobial activity,
and prevents infections, and closes wounds while stimulating healing. Saliva
also plays essential roles in food perception and digestion. The exact
mechanisms of digestion remain unclear. For taste, the physical and
compositional characteristics of saliva facilitate perception. For example, the
fact that saliva is an aqueous liquid makes it an ideal vehicle for carrying taste
stimuli and nutrients to the taste receptors which are widely distributed on the
tongue, soft palate, and pharynx. Unstimulated saliva also presents low levels
of taste stimuli, such as salts and glucose, in comparison to plasma, which
enables low detection threshold. Taste perception guides dietary choices as
well as influences physiological processes pre- and post-absorptivity. The
anticipatory phase of digestion is labelled the “cephalic phase responses” and
serves to prime the body to metabolize ingested nutrients efficiently, making it
an important step in food digestion and the prevention of deglycation and
dyslipidaemia.

6
Additionally, saliva contains many proteins involved in lipase, peptidase, and
hydrolase activities. When comparing the saliva and plasma proteomes, the
distributions of the salivary proteins are geared toward metabolic and
catabolic processes. This indicates that saliva has a major physiologic role in
food digestion. The most abundant protein in human saliva is the digestive
enzyme α-amylase [. This enzyme cleaves large starch molecules into dextrin
and subsequently into smaller malt oligosaccharides (MOS) containing α-D-
(1,4) linkages, sialyloligosaccharides (IMOS) containing α-D-(1,6) linkages, the
trisaccharide malt triose, and the disaccharide maltose. Glucose will then be
generated from maltose via the action of disaccharide enzymes, such as
maltase. In the human body, amylase is predominantly produced by the
salivary glands and the pancreas. Although salivary and pancreatic amylases
are similar, they are encoded by different genes (AMY1 and AMY2,
respectively) and show different levels of activity against starches of various
origins.

The physiological significance of salivary amylase is still being uncovered and

aspects of it are controversial, for example, its normative secretory function in
plasma remains a mystery. Salivary amylase has a relatively short active
contact time with starch. Once a food bolus is swallowed and infiltrated with
gastric juice, its catabolic activity is mostly stopped by low acidic pH. Some
activity remains within particles due to the barrier protection provided by
partially digested starch on the outside of the particle but most of the starch is
digested by the abundant pancreatic amylase, which is released into the
duodenal portion of the small intestine. Nevertheless, studies have
demonstrated that considerable starch hydrolysis occurs within seconds in the
oral cavity, transforming the gelatinous texture of starch into a semiliquid. This
change of texture might itself influence starch digestion, sensory preferences,
and starch intake. Additionally, recent studies have also demonstrated that the
small MOS amylolytic products can be detected in the oral cavity via the taste
system. These findings strongly support a physiological pre-absorptive role of
salivary amylase in starch digestion.

In this review, we will discuss the evolutionary forces that drive the existence
of salivary amylase, the benefits of generating higher salivary amylase levels,
the possible physiological consequences of early oral starch breakdown, and its
roles in protecting blood glucose profile and blood insulin, as well as the
disease states of metabolic syndrome, diabetes, and obesity.

7
Evolutionary Perspective on Salivary Amylase’s
Role in Starch Digestion
Salivary amylase has been detected in saliva of many omnivorous animals and
a few herbivores. In contrast, obligate carnivores, such as cats, never have
salivary amylase. Animals feeding on unripe fruits, seed, roots, and bulbs, all
rich in starch, exhibit higher salivary amylase activity. This supports the notion
that a key role of salivary amylase is starch digestion. Human salivary amylase
activity is by far the highest among primates. It has been attributed to the fact
that Homo sapiens possess multiple copies of the AMY1 gene, whereas the
other primates, including our nearest living relative the chimpanzees, display
the normative two copies per cell (one from each parent) . AMY1 copy number
variation (CNV) is not the sole driver of amylase production in animals, since
environmental factors such as stress level, circadian rhythms and diet
significantly contribute to quantitative variation among species and individuals.
Nevertheless, a good correlation exists between AMY1 copy number and the
amount and activity of amylase in saliva. Each duplicated segment of
the AMY1 gene contains the regulatory sequences necessary for salivary-
specific expression and thus can indeed directly influence messenger RNA
(mRNA) and protein expression levels. This is not the case of all gene-
containing CNVs. Humans can carry anywhere from 2 to 17 AMY1 gene copies.
High AMY1 copy numbers have been observed in populations in which
ancestors consumed diets rich in starch. this suggests a directional selection
toward higher salivary amylase for starch digestion. The development of
cooking and, more recently, greater access to starchy foods with the advent of
agriculture would have favoured AMY1 CNV, as the increased availability of
digestible starch would have resulted in salivary and possibly pancreatic
amylase levels becoming a limiting factor in starch digestion. It is important to
note that even if the pancreatic amylase genes in humans had not undergone
such extensive duplication, individual AMY2 CNV exists and varies from 0 to 4
for AMY2A and from 2 to 6 for AMY2B.

Like many animals, domesticated dogs, a non-obligate carnivore, only express

amylase in the pancreas and not in the saliva. Interestingly, wolves, which are
obligate carnivores, carry only 2 copies of AMY2B, whereas diploid copy
numbers in dogs range from 4 to 30; higher CNV is associated with increased
pancreatic amylase activity. This increase in amylase activity via duplication
of AMY2B is believed to explain why domesticated dogs can thrive on a diet
rich in starch, whereas its molecular mechanism (duplication) has acted on

8
similar genes in closest feral relatives cannot. Thus, the same different species
exposed to the same dietary pressure (domestication for dogs).

A parallel evolutionary event can be drawn between rodents and humans.

Rodents, like humans, possess salivary amylase. Studies have shown that both
species have acquired amylase activity in the saliva independently via the
insertion of a foreign retrovirus into the primitive amylase cluster, diverting a
pancreatic gene to become a salivary gene. Because this retroviral insertion
occurred after the separation of the primate and rodent orders, it implies that
some of the elements required for salivary amylase gene expression have
evolved independently in the mouse and human genomes. This supports the
idea of a very strong evolutionary selection for amylase to be excreted in
saliva. Those are striking examples of parallel evolution and strongly confirm
the importance of salivary amylase in starch digestion for humans. But the
questions remain, “What is this evolutionary pressure to express amylase in
saliva?” Or, “What does salivary amylase precisely do for us that conveys such
an advantage?” As the enzymatic activities of pancreatic and salivary amylases
are quite similar, and all mammals produce pancreatic amylase, there is no
obvious advantage to duplicate this starch digestion mechanism.

Pre-absorptive Role of Salivary Amylase in

Starch Digestion
Salivary amylase greatly impacts the textural characteristics of starch.
Enzymatic cleavage of starch produces a rapid decrease in glucose-polymer
chain length and viscosity after relatively few glycosidic bonds have been
cleaved. These changes in viscosity can play a significant role in determining
liking and preference for food. The degree to which the viscosity of starch is
thinned in the oral cavity could, therefore, be of nutritional importance. Our
group showed that individuals with high AMY1 copy number had a higher
salivary amylase activity and reported faster and larger decrease in perceived
starch viscosity than individuals with low AMY1 copy number. Improved
palatability of starchy food might have been one way that salivary amylase
CNV helped to increase starch consumption during hominid evolution. To this
point, people with ancestors who ate a more starch-rich diet carry higher
number of AMY1 CNVs.

Whereas starch does not have a clear taste to humans, oral detection of starch
or its degradation products via specialized taste receptors would be highly

9
beneficial because of its importance in the human diet. Considerable evidence
exists that rodents can orally perceive starch degradation products (oligo and
polysaccharides) and that their detection is independent of the sweet taste
receptor T1R2/T1R3. There is some evidence that people may also perceive
glucose polymers as having a distinct taste from that of sweet-tasting sugars.
Humans can discriminate the taste of high concentrations of maltose from the
taste of glucose or fructose when matched for intensity. More recently,
humans have been shown to respond to short MOS in the mouth as not sweet
tasting but perceptible. Thus, humans may perceive a weak glucose polymer
taste that is a unique quality of taste, distinguishable from sweet.

In addition, a T1R-independent metabolic pathway for monosaccharides has

been recently identified in taste receptor cells of mice. It consists of glucose
transporters (GLUTs) and a metabolic sensor pathway (sodium glucose
cotransporter 1 (SGLT1) and the ATP-gated K+ channel (KATP)) that serve as
metabolic sugar sensors in other tissues, notably the gut and the pancreas, and
may be a key step in the physiological differentiation between caloric and non-
caloric sweeteners. Thus, caloric sweeteners in rodents would act on two
signalling pathways, T1Rs and a metabolic sensor, whereas non-caloric sensors
would only act on T1Rs. The metabolic pathway could not explain by itself the
gustatory responses to starchy foods, since starch degradation products are
not substrates for GLUT or SGLT1 transporters, only glucose is transported, and
salivary amylase does not generate glucose. But this necessary step for the
metabolic detection of starch via the T1R-independent pathway in the oral
cavity has been identified as membrane bound disaccharidase enzymes. The
authors hypothesized that since gustatory and intestinal epithelia share many
chemoreceptors and signal transduction pathways (i.e., taste receptors in the
gut, metabolic sensors in the taste receptors cells) and since the enterocytes of
the intestinal epithelium express GLUTs and SGLT1 as well as disaccharide-
hydrolysing enzymes and contain pancreatic amylase, the taste cells may also
likely express those enzymes. They showed that taste cells express the
enzymes maltase-glucoamylase (MGAM), sucrase-isomaltose (SIS), lactase
(LCT), and trehalose (TREH), which hydrolyse the disaccharides maltose,
sucrose, lactose, and trehalose, respectively, to generate monosaccharides
that can be readily detected by GLUTs and SGLT1. They also showed
that AMY1 is expressed at low levels in taste tissue and at high levels in the
salivary parotid glands and lingual Von Ebner’s glands (VEG), confirming
previous findings. Thus, all the necessary machinery to elicit taste signals from
starch is present in the gustatory tissues. As VEG secrete their contents directly
into the trenches of the circumvallate and foliate papillae, VEG

10
produced AMY1 may be important in generating locally elevated number of
oligosaccharides and disaccharides in proximity of the taste pore where
MGAM, SIS, and GLUTs are localized, eliciting the metabolic signal even with
very low amounts of monosaccharides. It is interesting to note here that
Axelson et al., when comparing wolf and domestic dog genomes, reported
evidence for gain-of-function alterations in AMY2B gene and in the MGAM and
SGLT1 genes in dogs. so carbohydrate cleavage enzymes capable of generating
transportable monosaccharides can increase together during evolution.

In addition to conscious taste perception, gustatory activation stimulates

physiological responses (cephalic phase responses), such as increased
secretion of saliva, gastric acid, and pancreatic secretions. Such responses
prepare the digestive system to metabolize and absorb nutrients and enable
better maintenance of plasma nutrient homeostasis [. Cephalic phase insulin
release (CPIR) is one such pre-absorptive response to eating. Though it is a
relatively minor component of total insulin secretion, CPIR has been shown to
be an extremely important determinant of overall glucose tolerance. In one
study, our group showed that individuals with low salivary amylase activity due
to low AMY1 copy number did not exhibit CPIR in response to starch and
consequently had a higher glycaemic response. After ingesting a glucose
solution, those individuals, however, exhibited CPIR, which indicates that they
could do so. Those results suggest that salivary amylase may be important for
enhanced glucose tolerance and individuals with higher AMY1 copy number
better adapted to ingest starch. Recently, Glendinning et al. not only confirmed
that rodents possess two taste transduction pathways for sugars but also
demonstrated that if the T1R2/T1R3 pathway is required for attraction to
sugar, a pathway independent from T1R2/T1R3 mediates sugar-induced CPIR,
presumably the T1R independent metabolic pathway involving GLUTs, SGLT1,
and KATP and the carbohydrate-digesting enzymes in the case of di- or
oligosaccharide detection.

Therefore, starch break-down products released by salivary amylase can be

detected in the oral cavity and elicit an early release of insulin, possibly after
disaccharidases generate transportable monosaccharides. Via either or both
the metabolic taste pathway and the MOS taste pathway, the salivary amylase
activity in the oral cavity could improve starch metabolism pre-absorptivity.
Those pathways need to be confirmed in humans and the association between
high salivary amylase activity and starch-induced CPIR confirmed in larger
populations.

11
Post-absorptive Role of Salivary Amylase in
Starch Digestion
Large amounts of pancreatic amylase are released into the duodenum via the
pancreatic duct to continue the digestion of the incoming starch. The digestive
enzymes are produced and transported by acinar cells which are exocrine cells
of the pancreas. The second functional component of the pancreas is the
endocrine pancreas. The endocrine pancreas is composed of small islands of
cells, called the islets of Langerhans. The endocrine cells do not release their
secretions into the pancreatic ducts. Rather they release hormones, such as
insulin, into the blood to help control blood glucose levels. In a coordinated
manner, insulin directly regulates the acinar pancreas via a portal system that
conveys islet blood to acinar cells. The acini have insulin receptors, and it has
been demonstrated that insulin is necessary for normal acinar cell function.
Thus, insulin regulates pancreatic amylase secretion into the duodenum and by
extension starch digestion in the guts.

Curiously, amylase may not only serve exocrine functions but also have
endocrine functions as well. The presence of amylase in blood was historically
attributed to pathological leakage of pancreatic and salivary glands due to
inflammation and disease. The serum content of amylase would, therefore,
simply reflect the amylase content in the digestive glands: low in the case of
insulin deficiency and higher after feeding or after artificial activation of
exocrine secretion of the gastrointestinal glands. However, it has become clear
that the level of amylase in blood is in fact tightly regulated. So one must
wonder, what is its physiological secretory function? The presence of amylase
in blood results from a very active circulation process, a balance between rate
of entry and rate of clearance. When the parotid glands, a major source of
plasma amylase in rats, are removed, the resting level of salivary-type amylase
does not change, and an increase is still found to occur on feeding. Other
sources of the enzyme compensate their loss. One of the sources might be the
liver, which also produces low amounts of “salivary” amylase and can secrete
amylase into the plasma. Moreover, Cloutier et al. have demonstrated in rats
that circulating levels of amylase (and lipase) are related to their presence in
the intestinal lumen. Internalization by enterocytes and progression of the
absorbed enzymes along a transcytosis pathway allows them to reach the
blood circulation. In this study, amylase was present in higher concentrations
in the intestinal mucosa and in blood after feeding, as has been observed by
others. This type of internalization and transfer has not been studied for oral

12
epithelium; it would be interesting to know if it occurs in oral mucosa. Amylase
could serve digestive or nondigestive purposes in blood. The serum amylase
concentration is very low compared (ng per mL) with its concentration in
secretory glands (millimolar). Nevertheless, it is sufficient to detect enzymatic
activity and because of the high volume of blood (5 l) this concentration still
represents a substantial amount in the range of 1–10 % of tissue levels. It is
also possible that the circulation of amylase through the bloodstream provides
a means of transporting these proteins from one organ to another one. When
labelled exocrine pancreatic proteins were injected into the bloodstream of
conscious rats, the majority (approximately 97 %) were taken up by a variety of
body tissues, particularly kidney, liver, spleen, and lung.

Association between Salivary Amylase and

Obesity/Metabolic Syndrome
Recent studies have associated AMY1 CNV to obesity in European and Asian
populations. They found that increased salivary AMY1 copy number is
positively associated with lower body mass index (BMI) and obesity risk, thus
providing a genetic link between efficiency of starch digestion and low BMI,
due to the AMY1 gene. But other research teams have questioned those
findings, claiming that the authors used molecular methods, such as qPCR, that
are not able to provide a precise absolute count of CNV, leading to inaccurate
copy numbers at the AMY locus. When using methods with higher genotyping
resolution, the pattern of CNV at the amylase locus is very precise and differs
from the one obtained in the studies using qPCR. More importantly, they did
not observe the reported negative association between AMY1 and obesity or
BMI in large cohorts when using high resolution counting methods. Thus, it
appears that the effect of AMY1 CNV on obesity risk is not as strong as initially
surmised. Yet, the association is likely present nonetheless. Counts of gene
copy number and measurements of body mass are at opposite ends of the
spectrum of explanatory levels with a multitude of regulatory and
environmental factors intervening and diluting any causal link. Hence, it will
likely be difficult to find strong associations between salivary amylase CNV and
obesity. Also, the copy numbers of AMY1 and AMY2A are correlated, so that
phenotypic associations caused by variation in pancreatic amylase copy
number could be detected indirectly as an association with AMY1 copy
number.

13
At the protein level, low serum amylase has been observed for many years
within clinical settings in patients with obesity, type 1 and 2 diabetes, and
metabolic syndrome. Serum amylase consists of an almost equal proportion of
pancreatic and salivary amylase isoforms. Traditionally, serum amylase has
been measured by physicians to identify the presence of acute pancreatitis or
the degree of advanced chronic pancreatitis. Conversely, the exhaustion of
acinar cells and restricted flow of enzymes from pancreatic parenchyma into
the circulation or the destruction of β-cells, due to repeated pancreatitis, can
lead to low serum amylase as a result of low pancreatic amylase. Low serum
amylase has also been associated with an increased risk of cardiometabolic
disorders in large populations of asymptomatic adults. Obesity and diabetes
have a common pathology of insufficient insulin function, due to insulin
resistance and/or diminished insulin production, and insulin is known to be
critical to the production of pancreatic amylase. Therefore, low serum amylase
may reflect a manifestation of insufficient pancreatic insulin secretion in
asymptomatic people. Schneemann proposed that insulin resistance may
prevent the amplifying effect of insulin on amylase synthesis, leading to lower
amylase levels. Unfortunately, in almost all those studies and clinical
observations, only the total serum amylase was measured; so we do not know
what isoforms were present in serum. It would be very useful to differentiate
systematically pancreatic amylase from salivary amylase in blood. It is not
known if insulin has also a monitoring role on amylase produced by the salivary
glands or other salivary-type amylase producing tissues, such as the liver,
which makes small amounts of salivary amylase, but some studies point to a
causal insulin action on salivary amylase production in the salivary glands.
Thus, there may be a direct functional link between insulin function and
amylase production, thereby creating a causal link between starch digestion,
glucose homeostasis, and metabolic syndrome.

MATERIALS REQUIRED:
 Test tubes
 Test tube stand
 One dropper
 Beaker
 Stop watch
 Starch and Iodine solution
 Thermometer
 Dil. HCl and Dil NaOH solution.

14
 EXPERIMENT:
1.Collection of Saliva - Rinse mouth thoroughly with cold water and ensure that
it does not contain any food particles. Now take about 20ml of Luke warm
water in the mouth and goggle for about three minutes so that saliva mixes up
well with it. Spit this into a beaker. Filter, if there is any suspended impurity
clear filtrate is saliva solution and contains enzyme ptyalin.

2. Preparation of starch solution - Take about 0.5g of starch in a 100ml beaker

and add enough water to make a paste. Dilute the paste by adding 50ml water
and boil for about 5 min.

3. Digestion of starch
(a) take 5ml of the starch solution in a test tube. Add 2 ml of saliva solution
into it. Mix the solutions well by shaking the tube carefully and start a step
watch. (b) After one minute take out two drops of the mixture solution from
the test tube with the help of a dropper and transfer it into another test tube
containing about one ml of 1% iodine solution. Note the colour produced, if
any.
(c) Repeat this test after every one minute taking two drops of the mixture
solution and fresh 1% iodine solution continue until the test shows no blue
colour. Record the time and blue colour intensity.

OBSERVATION:

Time Passed after mixing 1 Min. 2 Min. 3 Min. 4 Min.

Colour Intensity Deep Blue Blue Light Blue No Blue

Absence of blue colour on addition to iodine solution means absence of starch

in the mixture solution. That is whole of the starch has got digested or
hydrolysed.

15
PROCEDURE:
Effect of temperature on the digestion of starch by saliva

 Take three test tubes and label these 1, 2, 3.

 Take 5ml of the starch solution, 2ml of the saliva solution and 5 ml of
water in each test tube.
 Place test tube No. 1 in water at room temperature, test tube No.2 in a
beaker containing water at 500 C and test tube No.3 in boiling water.
 After 5 minutes, observe the colour change on mixing two drops of the
mixture of every tube with one ml of 1% iodine solution. Note the
intensity of blue coloured form.

CONCLUSION:

Starch gets hydrolysed by saliva amylase.

PROCEDURE:
To study the effect of pH on the salivary digestion of starch

1. Take three test tubes and label these 1, 2, 3.

2. Add 5ml of the starch solution, 2ml of the saliva solution in each test
tube.
3. Now add 2 ml of water inn test tube No. 1, 2 ml of dil HCl in test tube
No. 2 and 2ml of dil NaOH solution in test tube No. 3 and shake carefully.
4. Keep the three test tubes in water at room temperature for about 10
minutes.
5. Add two drops of the solution of each test tube with 1% iodine solution
and observe the colour change.

CONCLUSION:

Temperature effects the digestion of starch by saliva with increase in temp

salivary analyse get inactivated and process of digestion do not take place.

16
 CONCLUSION:
Salivary amylase affects oral perception of starches, pre absorptive metabolic
signalling, and plasma glucose responses to ingested starch. These early
controls of digestion result in differences in the efficiency with which starch is
handled metabolically. These metabolic controls appear to be of sufficient
importance that the pancreatic amylase gene has been copied and expressed
in the salivary glands in primates and in rodents independently. In humans,
who since the advent of agriculture greatly increased starch intake, the salivary
amylase gene has greatly expanded as a copy number variant. Yet, in modern
society people tend to eat the same amounts of starch on average whether
they make high or low levels of salivary amylase. This appears to put those
who produce low levels of salivary amylase and eat high amounts of starch at
risk for developing metabolic syndrome.

17
EVIDENCE:

18
 BIBLIOGRAPHY:

1. https://www.olabs.edu.in/?
sub=79&brch=18&sim=236&cnt=1#:~:text=How%20to%20test
%20it%3F,and%20converts%20it%20into%20maltose.
2. https://www.toppr.com/ask/question/study-of-digestion-of-starch-
by-salivary-amylase-and-effect-of-ph-and-temperature-on/
3. https://www.allprojectreports.com/CBSE-HBSE-School-Projects/
Chemistry-Project-Report/Chemistry-Project-Digestion-Starch-
Salivary-PH-Temperature.htm
4. https://www.allprojectreports.com/CBSE-HBSE-School-Projects/
Chemistry-Project-Report/Chemistry-Project-Digestion-Starch-
Salivary-PH-Temperature.htm
5. https://www.academia.edu/35779243/
To_Study_the_digestion_of_starch_by_salivary_amylase_and_effe
ct_of_temperature_and_pH_on_it

19