Ph Buffers To Amylase On The Rate Of Starch

Ph Buffers To Amylase On The Rate Of Starch
Research Question: What is the affect of adding different pH buffers to amylase on the rate of starch
digestion measured using starch and iodine?
Background information:
pH is a measure of the concentration of ions in a solution. In other words, concentration of H+ and
OH molecules compose pH. When the concentration of H+ and OH ions are balanced (equal), the
solution is considered neutral. When the H+ dominates the OH molecules, the solution is considered
acidic. When the OH dominates the H+ molecules, the solution is considered basic.
Buffer is to be able to add either strong acid or base to a solution avoiding a great change in the pH.
Iodine is a significant element for life commonly needed by living organisms. Amylase is an enzyme
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This mixture of amylase and pH buffer will be modified by the addition of more pH buffer into
water down (diluted) amylase enzyme. Also, the pH buffers used in this experiment vary by 1, 4, 7,
10 and 14.
Dependent Variable: Rate of starch hydrolysis, which will be determined by the change of color; if
the iodine turns blue– black it indicates that the enzyme is denatured and if the iodine turns orange–
yellow it indicates that the enzyme is working properly by digesting the starch.
Controlled Variables:
Amount of iodine. 50µL of iodine will be equally added into each micro plate.
Amount of starch and amylase mixture. 5ml of starch solution and 500µL of enzyme solution
composed of amylase and pH buffer.
Temperature. The experiment will be maintained in the lab at temperature (30°C)
Uncontrolled Variable:
Microorganisms might get in the tubes. To reduce this pollution, I will have to clean the lab
beforehand.
Sunlight may slightly disturb the maintenance of the room temperature.
Apparatus:
pH buffer (1,4,7,10 and 14)

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Effect Of Amylase On Bread
THE EFFECT OF AMYLASE ON BREAD
What is bread? Bread is a food made of flour, water, and yeast mixed together and baked. In bread
making, our main focus will be on the enzyme amylase. In wheat, there is naturally appearing
amylase. Amylase in the shape of malted barley can be mixed with flour in minor amounts to
achieve a proper balance of enzymes. The key purpose of amylase in wheat flour is to break down
complex starches into simple sugars. Without this key process happening in the dough, fermentation
would not occur because yeast needs simple sugars in order to make carbon dioxide. A proper
balance of natural amylase in wheat flour is needed in order to make bread that is accurately
fermented with a good colored crust and well–developed flavor. ... Show more content on
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Numerous enzymes are needed in dough to break down starch into simple sugars that yeast can
digest. The process is a very complex one, and includes the enzymes alpha amylase and beta
amylase. Starch occurs in two different forms, a branched form called amylopectin and an
unbranched chain called amylose.
The dough must contain some alpha amylase to be able to digest the portion of starch that is
amylopectin. If the alpha amylase is too much in the dough the starch will completely liquify. Alpha
amylase attacks starch virtually wherever along its chains, producing smaller chains of different
lengths. These chains can hold smaller units called dextrin's that contain numerous units of glucose.
Beta amylase can then digest these dextrin's into maltose.
Flour always has a suitable supply of beta amylase that can digest amylose totally into sugars. Beta
amylase attacks amylose the chains and breaks them into molecules of maltose. Maltose is a
disaccharide (A disaccharide is the sugar formed when two simple sugars are joined by glyosidic
linkage) containing two glucose

Amylase Temperature
This experiment was performed to demonstrate how varying temperatures affects the activity of the
enzyme, amylase. Also, it was conducted to determine the optimal temperature for the fungal,
Aspergillus oryzae, and bacterial amylases by placing them both into different test tubes with
differing temperature conditions. At varying time intervals, both enzymes were removed from their
assigned temperatures. A drop of each enzyme will then be placed on two different spot plates with a
pipette. All the wells on the spot plates contain three drops of iodine to clearly show whether a
reaction has taken place. The pipette was used to mix the iodine with the starch enzyme to organize
the levels of starch catabolism based on temperature. At the end of ... Show more content on
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Amylase is the enzyme that catabolizes starch polymers into maltose which is a saccharide, or sugar,
used as a food source and to store energy. In addition, both starch and amylase are essential in the
commercial production of syrups, other food products and brewing processes (Alberte, Pitzer,
Calero, 2012). Although, it is important to know the optimal temperatures of both enzymes, it is also
important to know that this is not the only factors that affects the activity of the enzymes. Substrate
concentration, salt concentration, and pH level are affect enzymatic activity. The presence of
inhibitors, or molecules that bind to an enzyme decrease its activity, while activators increase
enzymatic activity. If the temperature of an enzyme is greater than the optimal temperature, the
active site of that enzyme denatures. In other words, it changes shape, which will prevent substrate
binding. Without the substrate binding, the enzyme will not be able to carry out its normal functions
and this can lead to a deficiency of an enzyme. In this case, if there were insufficient amylase in
human body, it can cause cystic fibrosis, celiac disease, or Crohn's

How pH Affects the Break Down of Starch by the Enzyme...
How pH Affects the Break Down of Starch by the Enzyme Amylase
Hypothesis:
The optimum pH for the reaction of starch with amylase is pH 7. PH values lower or higher than this
value will result in a slower rate of reaction. Amylase works in the range pH 3 to pH 11.
Biological Knowledge ====================
PH changes affect the structure of an enzyme molecule and therefore affect its ability to bind with
its substrate molecules. Changes in pH affect the ionic bonds and hydrogen bonds that hold the
enzyme together, which naturally affects the rate of reaction of the enzyme with the substrate. On
top if this, the hydrogen ions neutralise the negative charges of the R groups in the ... Show more
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7 Corvettes
These are used instead of test tubes as corvettes are required if a colorimeter is to be used. One
corvette is needed for each pH and one for the control. These can then be reused for the repeats.
Syringe calibrated at 0.1 cm³ intervals
This is vital to measure out the volumes of the starch and amylase solutions accurately using these
calibrations to achieve precision. This apparatus is far more accurate than using a measuring
cylinder, as there are minimal transference losses.
2 Syringes
As the volume of buffer solution of iodine is not being measured, only the number of drops,
apparatus with calibrations is not required for this.
Stopclock
This is important for measuring the time. It is not important whether a digital or traditional
stopclock is used as there will be the same percentage error either way.

Method
* Measure out 1 cm³ amylase solution with calibrated syringe and put in corvette
* Add to this 5 drops of pH 4 buffer solution
* Measure out 2 cm³ starch solution
* Start stopclock and leave for 1 minute
* Measure out 1 cm³ amylase and place in second corvette
* Add to this 2 cm³ distilled water
* Add 3 drops of iodine solution
* Shake it well,

Amylase Lab Report
Structure and Function of Amylase
ABSTRACT:
Animals intake large amounts of carbohydrates for energy as part of their daily diet. These
carbohydrates are composed of sugars or joined glucose units. To study how animals tissues derive
energy from these sugars, enzymes such as amylase have to be studied. amylase is an
enzyme that breaks down starches into simple sugars. By identifying the components of amylase
and determining their functions, one was able to better understand the overall function of
amylase and consequences of not having certain components of amylase or a deficiency in
the amylase enzyme. The study showed that a direct relationship between a deficiency in an
enzyme and disease has not been identified.
INTRODUCTION:
Carbohydrates, a major part of an organism's diet, contain long and branched chains of glucose.
Those glucose monomers are joined through  linkages or  linkages to make up
starch. For an organism to extract nutrients and energy, starch has to be broken down into simple
sugar molecules such as maltose as shown in Figure 1. Maltose, for example, can then be absorbed
into the blood as a small, soluble chemical. For this to occur, starches have to go through two types
of digestion, mechanical digestion and chemical digestion. Mechanical digestion is the physical
breaking of food into smaller pieces using an organism's teeth and muscles, while chemical
digestion is the breaking of food using acids and enzymes. Since mechanical

Enzyme Kinetics Lab Report: The reaction rate of enzyme,...
Abstract:
This experimentation was to evaluate absorbance and the reaction rate of an enzyme, '–amylase in
starch–iodine solution. We will be testing the relationship between enzymatic reaction affected by
temperature and pH. Through the testing the enzyme at different temperatures, and different pH
levels; it would determine at which temperature and pH level the enzyme worked the most
efficiently. Analyzing absorbance of the solutions with spectrophotometery will determine the
reaction rate.
To test the optimal pH, the starch and a buffer were combined at a specific pH level and tested the
absorbance of a solution at various times. To resolve the reaction rate of a solution at various
temperatures, the solution was put into water both ... Show more content on Helpwriting.net ...
Before the proceeding of an experiment, makes sure the spectrometer turned on for at least 15
minutes to be warm. After turning on the spectrometer set the wavelength at 560nm. Add '–amylase
to starch–iodine solution. To examine the starch–iodine solution at different pH levels, a 35mL stock
starch and 35mL of buffer at pH level 4.5 were placed into an Erlenmeyer flask to set up the reaction
flask solution. Adjust spectrophotometer with mixture of 5mL of distilled water and 0.1mL of the
starch iodine in cuvette (the blank). Turn the transmittance knob and set the line at zero. Place the
ready blank solution into the spectrophotometer and turned the absorbance knob and set the line at
zero. Then added 0.1mL of the I?'KI indicator into the cuvettes.
Record the first data at 0 minute, add 5mL of the solution from the reaction flask into a cuvette with
I?'KI indicator in it. Then placed cuvette into the spectrophotometer and recorded the absorbance.
After recording the initial absorbance at 0 minute the TA put 1mL of '–amylase solution into the
reaction flask then began to time the experiment. Every two minutes 5mL of solution was put into
starch–iodine solution. The absorbance was recorded every two minutes for 20 minutes. After
recording the absorbance of 35mL of distilled water and the 35mL buffer at a pH of 4.5,

The Effect Of Ph On The Function Of The Enzyme Amylase
Discussion – Effect of pH on the Function of the Enzyme Amylase
The objective of the lab was to examine the effects of environmental variables on the functions of an
enzyme. To the point, an experiment was conducted to test the effect of pH on the function of the
enzyme Amylase. Enzymes are proteins that act as catalysts and help reactions take place. In short,
enzymes reduce the energy needed for a reaction to take place, permitting a reaction to take place
more easily. Some enzymes are shape specific and reduce the energy for certain reactions. Enzymes
have unique folds of the amino acid chain which result in specifically shaped active sites (Frankova
Fry 2013). When substrates fit in the active site of an enzyme, then it is able to catalyze the reaction.
Enzyme activity is affected by the concentrations of the enzymes and substrate present (Worthington
2010). As the incidence of enzyme increases, the rate of reaction increases. Additionally, as the
incidence of substrate increases so does the rate of reaction. Almost all enzymes need specific
conditions for them to function. The conditions include temperature, pH level, and concentration of
salt. Enzymes have optimal conditions. If they are changed, the enzyme may denature and
deactivate. If that happens, the enzyme would not be able to catalyze the reaction, and the reaction
rate would decrease (Worthington 2010). Amylase is a digestive enzyme. The enzyme is found in
the salivary glands in your mouth

Amylase Enzyme Lab Report
The amylase enzyme is one that is essential in the human digestive process, as it breaks down larger
molecules in the body to make sure that these molecules can be digested more easily. More
specifically, the amylase enzyme is most commonly found in human saliva and in the pancreas,
where it preforms the pivotal function of breaking down of starch into monosaccharides.
When starch is mixed with iodine, the beta amylose molecules found in the starch trap iodine,
causing the mixture to turn a bluish black color (Senese, Fred). However, when the starch is broken
down into glucose, the substance does not react to the iodine, resulting in the glucose in the mixture
not changing color. Additionally, when amylase is mixed with a bluish black mixture

Undigested Starch Lab
In Table one the solution remained brown since there is no starch present in the mixture in tube
1A.The solution turned blue black due to presence of starch in the solution in tube 2A.The solution
remained brown since there is no starch present in the mixture in tube 3A.The solution turned blue
black due to presence of undigested starch in the solution. Boiling amylase denatures the enzyme
hence it cannot digest amylase in tube 4A.The solution remained brown since there is no starch
present in the mixture. All is digested in tube 5A.In tube 6A the solution turned blue black due to
presence of undigested starch in the solution. The extremely low temperatures inhibit the action of
the enzyme amylase. There was no presence of maltose in tube ... Show more content on
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It formed an orange color. There was no presence of maltose in tube 4A. Starch was also undigested.
In tube 5A Maltose was present in the solution as a result of digestion. It formed an orange color. In
tube 6a there was no presence of maltose. Starch was also undigested.
In table two there was no hydrolysis present in tube 1T.There was also no protein available in
mixture. There was no hydrolysis present in tube 2T. There was also No trypsin available in mixture
in tube 3T there was no hydrolysis was present .Trypsin was also denatured by boiling. In tube 4T
there was Hydrolysis present. All conditions were optimal for digestion. In tube 5T there was no
hydrolysis present. The Temperatures was too low for enzymes to operate.
In table three in Tube 1L there was no lipase action present. Also there was not any fat present in
mixture. In tube 2L there was also no lipase action nor any lipase present in mixture. In tube 3L
there was no lipase action. Lipase was denatured by boiling. In tube 4L there was Lipase action
present. All conditions were favorable. In tube 5L there was not any lipase action because the
temperatures were too low. In tube 4B Lipase action was present. All conditions were favorable and
bile salts accelerated the digestion. In Tube 5B there was no lipase action because the temperatures
were too

Porcine Pancreatic Alpha Amylase
The Effects of pH levels on Porcine Pancreatic Alpha Amylase Activity in a 1% Starch Solution
Introduction
Enzymes are protein complexes which lower the amount of energy needed to complete chemical
reactions in cells, and therefore, increase the rate of chemical reactions. Without enzymes, chemical
reactions in the body would occur at much slower rates, they are critical to cell function. The
enzyme used in this experiment, alpha–amylase, is a catabolic enzyme found in two places within
the body: the pancreas and salivary glands. A catabolic enzyme, such as amylase, breaks down
complex organic molecules into simpler substances. Amylase fits the description of a catabolic
enzyme because of it's ability to catalyze the breakdown of starch, ... Show more content on
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The body must keep pH levels of organs at their optimal levels in order for their enzymes to
function. If a pH level strays from optimal, the enzyme will become denatured and will no longer be
able to catalyze reactions. Alpha–amylase function is also important for companies in the starch
industry. These companies use this starch hydrolyzing enzyme in various fields such as food, textile,
paper, baking, and detergent (Gregory & Woods, 1995). It is important for these companies to know
what pH level is optimal for amylase to be highly functional and in turn, efficient for their
companies. Perhaps future studies in the exact structure of the enzyme pancreatic alpha amylase will
help scientists understand how to manipulate pH levels within the

The Role Of Bella In Her Pet Cheeseburger Ebenezer
Bella is in a fight with her pet cheeseburger Ebenezer because he got ketchup all over her new white
shirt. Though in the end, she concludes to solve her problem by eating him. Primarily, Ebenezer, the
cheeseburger, enters the digestive tract through the mouth in which he is cut, torn, and grinded into
pieces through mechanical digestion, in which Bella can swallow by her teeth. Bella's saliva then
helps her soften, moisten, and break down the starches of Ebenezer so that she is ready to swallow
him. This is when ingestion happens or the process of taking in food. In swallowing Ebenezer, Bella
closes a trap door in her throat known as the epiglottis. Suddenly, Ebenezer is in her pharynx, which
hands him to her esophagus, which carries him to

Amylase Lab Report
Abstract
This report will explore the possible gene copy variation that can occur in the AMY1 gene that
produces amylase, which breaks down starch. This variation is likely to occur to individuals that
have ancestors with high starch diets. It is hypothesized that individuals with high starch diets, have
a duplication of the AMY1 gene (Tracey 2016). As an individual with family eating a high
rice/starch diet, I would hypothesize to have this variation. This study will be completed through
collection of individual saliva, and put through a polymerase chain reaction to determine the
amylase concentration and the gene copy number. It was evident, that this variation is not very
common, and did not support the hypothesis, as my gene copy number was one.
Introduction
Amylase is the enzyme that is found in saliva that is responsible for breaking down food such as
starch and glucose. This enzyme is able to catalyze the hydrolysis of starches into glucose. The gene
responsible for the production of amylase is AMY1A, officially known as amylase, alpha 1A(Tracey
2016). The level of salivary amylase enzymatic activity is variable among each individual (Mendel
et al 2010). It is hypothesized that ancestral starch consumption reflects the gene copy number of the
gene AMY 1 in consecutive generations (Tracey 2016). It is ... Show more content on
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Amylase concentration, the equation is y= 0.0382x – 1.0162. The R2 value is 0.92732. Serial
dilutions were made using individual saliva, with measurements of 10x, 100x, and 1000x. From
these dilution factors, the closest number to the absorbance curve was 1.4829ug/mL, which is my
amylase concentration in saliva. During lab 6, the amylase saliva DNA was put into a PCR chain
reaction and then in lab 7 it was put into a gel electrophoresis. The amylase moved 38mm along the
100bp ladder. The adj. volume for amylase fragment was 730, 010 actin adj. volume was 632,704,
which determined that my gene copy number was

Amylase Lab Report
The results in Figure 1, supported both the hypothesis as well as the predictions because the graph
depicts how the differences in temperature changed the enzyme activity of amylase. The results
concluded that as temperature deviates from optimal temperature amylase will hydrolyze starch at a
lower rate. At 5 and 70 degrees Celsius amylase took longer to hydrolyze starch compared to 25 and
40 degrees Celsius. The results also supported the prediction that at 40 degrees Celsius, enzymes
will break down starch at a faster rate than at 5 degrees Celsius, 25 degrees Celsius, or 70 degrees
Celsius. The results showed 40 degrees Celsius as the optimum temperature for the hydrolysis of
starch because 40 degrees Celsius is close to the body's temperature. Amylase denatures at 70 to 80
degrees Celsius which causes the enzyme to become damaged and can no longer hydrolyze the
starch. The results of this ... Show more content on Helpwriting.net ...
Living organisms are dependent on the use of enzymes to speed up biochemical reactions. Enzymes
will catalyze one specific chemical reaction since they have a unique three dimensional shape that
allows one substrate to bind to the active site. The enzyme Amylase is found in human saliva that
speed up the hydrolysis of starch into smaller carbohydrate molecules. When humans are sleep
deprived there is an increase in amylase and this study done by Räikkönen shows that short sleep
duration in both children and adults correlates to an increase in amylase. Compared to girls, boys
were found to have a lower efficiency and shorter duration of sleep compared to girls. This study
offers insight on how poor sleep is associated with poor health because children and adults with high
levels of the enzyme amylase also have an increase in stress. . Further testing could lead to a better
understanding of how sleep–wake cycles and their genetic makeup affects the enzyme amylase
production. (Räikkönen et al.,

The Effect Of Amylase Concentration On Human Population
1.0 Introduction
With the constant integration of technology into human households, it is apparent that biological
enzymes such as the alpha amylase are to be implemented into sanitary procedures. One such
example lies within the utilisation of enzymes in laundry detergents. Enzymes have recently assisted
the development and improvement of modern household and industrial detergents (Journal of
surfactants and detergents 1998). The alpha amylase is essential in hydrolysis of starch molecules,
as it catalysis splits in starch so that they consist of short chains of glucose units. These units can
then be broken down by water allowing it to dissolve into the solution. Though the limitation
associated with the alpha amylase is that excess concentrations cause odours to be trapped within
clothing material. Additionally due to the presence of alkalis in laundry detergents it can cause an
altering of pH, thus affecting the ability of the enzyme to catalyse reactions. Hence in order to
understand the most optimal conditions for cleaning, this investigation will analyse the effects of
amylase concentration within altering pH solutions to determine the best solution to aid in stain
removal. The investigation will utilise fungal amylase, which is essential in replicating factory
amylase which is implemented into house hold detergents.
1.2 Aim
The aim of this investigation was to analyse the effects of altering pH and amylase concentration in
starch removal in order to verify

The Digestive Enzyme Amylase
The digestive enzyme amylase was analysed in two different species of gastropod (the herbivorous
Turbo smaragdus and the carnivorous Cominella adspersa), in order to assess whether diet
influences digestive enzyme activity. This was determined by preparing a tissue homogenate from
the digestive gland of each of the species and comparing their measured absorbance to that of a
standard curve that reflected the relationship between absorbance and enzyme units.
Amylase activity (in units of enzyme per gram) was significantly higher in the herbivorous species
than in the carnivorous species, yet there was wide disparity in activity within the species –
indicating a degree of plasticity in the enzyme's activity. The difference between T. smaragdus and
C. adspersa does, however, indicate that the activity of amylase follows a pattern influenced by diet
in these species.
Introduction
Most animals possess digestive enzymes that allow them to digest the food they consume. There is,
however, variation between species in the activity of individual enzymes (Chan, et al. 2004;
Chakrabati, et al. 1995), and this can indicate feeding ecology in animals. For instance, Kuz'mina
(1996) found that certain digestive enzymes were correlated with diet composition: amylase
activities were lowest in carnivorous species of fish and highest in herbivores. Hence, the
physiological requirements to live as a carnivore or herbivore certainly differ between families.
Not only is this effect apparent in

How Carbonated Water Affects The Production Of Amylase By...
Almost everyone has sat down on their couch, turned on the T.V., and sat there for hours, eating
chips and drinking soda. It may have never occurred to people that, when they do this, a chemical
reaction is being catalyzed in their mouths by the enzyme "amylase." This chemical reaction
happens all the time, but with soda in the mix during this reaction, the outcome could be different.
This experiment will test how carbonated water, like that of soda, affects the production of sugars by
breaking down starch through amylase. Amylase is an enzyme that breaks down plant starches into
simple sugars like glucose. There are many types of amylase, but the one found in humans' saliva is
alpha–amylase. Alpha–amylase breaks up polysaccharide bonds within the starch molecules – by
using water – in order to reduce them to glucose. This breaking up is called hydrolysis. The alpha–
amylase ... Show more content on Helpwriting.net ...
This project expands on previous research by providing a direct connection between carbonated
water and amylase's production of glucose. Now, the only information found connecting these topics
is that they both aid in digestion. In this project the effect of carbonated water on the production of
glucose by amylase will experimented to different degrees. The independent, manipulated variable
is the amount of carbonated water and the dependent, responding variable is the amount of glucose
produced by amylase. Various percentages of a carbonated water and water solution, including just
water and just carbonated water, will be combined with starch to make many different solutions.
Amylase will be poured into each of those solutions and then, the amount of glucose created from
the hydrolysis of the starch in the solution will be recorded. This will show what the effect of
carbonated water on the production of glucose by amylase

The Effect Of Temperature On The Enzyme Amylase And Its...
When the experiment was conducted, the main objective was to determine how temperature affected
the enzyme amylase and its activity. The function of amylase in this experiment was to break down
or digest starch into smaller molecules. In the context of the experiment, the amylases function was
to break down starch into monosaccharides. As defined in the Biology in Focus textbook written by
Urry, Cain, Wasserman, Minorsky & Reece, monosaccharides are defined as simple sugars of the
macromolecule carbohydrate, which are consumed by humans and other organisms (p. 49). The
objective of the experiment was to establish if there was a correlation between the temperature and
the enzyme's activity or if there was no correlation between temperature ... Show more content on
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51). The importance of the types of amylases that were used were significant when examining if
they were able to break down starch or not because if the enzymes' function differed from what was
being tested nothing would occur. In the academic article "Experiments on the Amylase of
Aspergillus oryzae" by Arthur Tangerg, he mentioned that Aspergillus oryzae was able to convert
starch into glucose, which was crucial in this experiment as the enzyme's function correlated to what
was being tested (1915, p. 34). This type of fungal amylase was a good candidate to test on because
of its ability to break down starch. Since the enzyme's function was to break down starch it would be
clear when determining its optimal temperature that it was able to digest starch. In the study
"Biodegradation of food waste using microbial cultures" written by Awasti et al. (2017), the
bacterial amylase, Bacillus Licheniformis, was used due to its high enzyme activity as well as its
ability to resist a range of different temperatures (para.5). The importance of studying the effects of
temperature on the fungal and bacterial amylase was to determine under which conditions were the
enzymes capable of carrying out their function. Since the enzymes were not extremophiles, the two
extreme temperatures 0o Celsius and 86 o Celsius could be

Salivary Amylase And Phosphorylase
Introduction
The purpose of this experiment was to determine the enzyme activity for salivary amylase and
phosphorylase by placing them under different conditions of temperature and enzyme concentration.
An enzyme is a protein that acts as a catalyst to form reaction, and see the activity of the specific
enzyme (Knowles, 1991). One part of the enzyme, salivary amylase, is that alpha amylase is in the
saliva of most animals because this enzyme breaks down starch (Jacobsen, Melvaer, Hensten–
Pettersen, 1972). In the presence of starch, this enzyme is present in saliva, but is not present when
there is no starch present (Jacobsen, Melvaer, Hensten– Pettersen, 1972). The conditions for salivary
amylase to have a reaction with starch would change in temperature and enzyme concentration, as
well as, monitoring the pH levels (Jacobsen, Melvaer, Hensten– Pettersen, 1972). Salivary amylase
is an enzyme is human saliva that helps in digestion of specific substrates, such as starch (Hudman,
Friend, Hartman, Ashton, Catron, 1957). It breaks down starch molecules by splitting maltose from
the non–reducing end of a gluten molecule (Jacobsen, Melvaer, Hensten–Pettersen, 1972).
Phosphorylase acts on starch and glycogen by breaking it down by breaking the glucose bonds and
taking a glucose molecule off of the structure (Ball, Vialle, Alonso–Casajus, Duavillee, Munoz,
Baroja–Fernandez, Moran–Zorzano, Eydallin, Pozueta–Romero, 2006). The conditions for the
reaction of Phosphorylase and

Correlation Between Regional Gene Evolution
Through the process of this study, students intended to illustrate the presence, or lack thereof, of an
affiliation between regional gene evolution, globular gene copy number variation, and individual
protein production status (Tracey 2017). It was hypothesized that the student's ancestral diet
included relatively high levels of starch–rich foods; thus the number of amylase, alpha 1 (AMY1)
diploid gene copies that they retained and their production of the amylase enzyme would be
significantly higher than the mean values of the students as a collective. The students followed the
procedural guidelines of the Winter 2017 Biology 1A03 Laboratory Manual with minimal
procedural modifications made (Tracey 2017). It was revealed that the student, ... Show more
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In order to evaluate this hypothesis, the student had to compute their exact salivary amylase
concentration –as measured in milligrams per millilitres, – the number of amylase gene copies
encoded in their DNA, and their ancestral dietary starch consumption. Ultimately this would aid in
determining whether a correlation exists amongst genome evolution within populations, individual
gene duplicate numbers and protein concentrations (Tracey 2017).
For the protocols employed throughout the study refer to the Winter 2017 Biology 1A03 Laboratory
Manual, experiments two through eight (Tracey). Let it be noted that severely alterations were made
to these procedures. During experiment four, the salivary samples were centrifuged for a total of
sixty seconds rather than five as per the discretion of the teaching assistant (Tracey 2017).
Moreover, the directions for experiment six required students to pipet ten microlitres of their buccal
samples into a polymerase chain reaction (PCR) tube but did not account for the fact that the
micropipette tips would not fit into the samples tubes (Tracey 2017). Thus, students poured small
quantities of the culture into a microcentrifuge tube first and then measured out the ten microlitres
from there. Finally, while the script for experiment

Optimal Temperature Of The Fungal Amylase
Ramos 2
Abstract
The purpose of this experiment was to come up with the optimal temperature of the Fungal
Amylase, Aspergillus oryzae, and the Bacterial Amylase, Bacillus liceniformis, as well as to identify
if different temperatures would indeed affect the enzyme amylase by either slowing down the
process or denaturing the enzyme. Enzymes are complex proteins, they can be thought of as a
substance fabricated by a living organism that behaves as a stimulus, otherwise known as a catalyst,
to cause a specific biochemical reaction. This experiment was performed by keeping the amylase
mixed with starch at different temperatures, either in the heated water or in the ice bath. The
temperatures varied at either 0, 25, 55, or 85 degrees Celsius. After a certain amount of time we
would then move the test tubes containing the amylases and position them on a plate where iodine
was then added to the starch amylase solution. We would do the same thing at different time
intervals to see exactly how the enzyme catalyzed the starch. The hypothesis of this experiment was
thought to be that the higher the temperature the slower the enzyme would then hydrolyze the
starch. Both the Fungal and the Bacterial Amylase had an optimal temperature of 55 degrees Celsius
as shown by our concluded results in this

Amylase Is An Enzyme Commonly Found In Human Saliva. It
Amylase is an enzyme commonly found in human saliva. It is used to catabolize starch into glucose
and maltose by lowering the activation energy barrier, and by breaking the alpha 1–4 bonds of
amylose and amylopectin and the alpha 1–6 bonds of amylopectin. Amylase is found in one's saliva
and pancreas, and Porcrine Pancreatic α–Amylase is amylase that has been isolated from the
pancreas of a pig. While amylase is effective at breaking down starch, in the normal saliva pH range
of 6.02 to 7.14 (Schmidt–Nielsen, 1946), any pH environment outside of this range will decrease the
reaction rate. The same goes for the temperature of the amylase's environment. At a normal body
temperature of around 37°C, the amylase functions at its fastest rate ... Show more content on
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Through this experiment we found this prediction to be true; even though there is no true consensus
on the exact optimum pH for alpha–amylase activity, all of the sources place it around 6.00 or 7.00.
Materials and Methods First, six different buffers were used and 5 mL of each buffer was added to
six different test tubes. The six buffers were as follows: pH 4.00 was Potassium Biphthalate (Item #
280–4.00), pH 5.00 was Potassium Biphthalate/ Sodium Phosphate (Item # 280–5.00), pH 6.00 was
Potassium Phosphate/ Sodium Phosphate (Item # 280–6.00), pH 7.00 was Sodium Phosphate/
Potassium Phosphate (Item # 280–7.00), pH 8.00 was Sodium Phosphate/ Potassium Phosphate
(Item # 280–8.00), pH 9.00 was Sodium Bicarbonate/ Sodium Carbonate (Item # 280–9.00). All of
the aforementioned hydrion buffer salts were obtained from Micro Essential Laboratories in
Brooklyn, NY. Secondly, 1.5 mL of a 1% w/v α–Amylase solution from porcine pancreas, Type VI–
B, ≥10 units/mg solid, from Sigma–Aldrich in St. Louis, MO, (Item # A3176–500KU) was added to
each test tube, and the solutions in the test tubes were mixed. Next, 100 μL of 2% Iodine Solution,
I2KI, from Carolina Biological Supply Company in Burlington, NC (item # 869093) was put into
wells in several rows of seven different

A Biological Catalyst Essay
A Biological Catalyst A Biological catalyst is a catalyst that is produced organically. In other words,
a cell makes it. It is usually a protein or steroid molecule that works to catalyse a specific reaction.
For example, amylase is a biological catalyst. Biological catalysts are called enzymes. Reactions
take energy to get them started. This energy is called the activation energy. Enzymes catalyse
reactions inside organisms. A catalyst is a molecule that acts as a matchmaker, bringing together the
chemicals of the ... Show more content on Helpwriting.net ...
Salivary amylase is an enzyme that breaks down big molecules into smaller ones. Amylase enzyme
breaks starch molecules up into two–residue units (a residue is a glucose molecule, or 'monomer' of
sugar. Lots of residues joined together form a polysaccharide. Starch is a polysaccharide). Two
glucose molecules split off from the starch molecule form maltose. This maltose is the product of
catalytic action by the enzyme amylase on the substrate. The substrate is the starch.
2.) What are intracellular/ extracellular enzymes? Enzymes are proteins. They are very important
substances because they control the chemical reactions that happen in our bodies. There are two
main types of enzyme. Digestive enzymes are extracellular enzymes – they control reactions that
take place outside cells. Those enzymes that control reactions inside cells are called intracellular
enzymes.
3.) What is the Lock and Key theory? The lock is the enzyme and the key is the substrate. Only the
correctly sized key (substrate) fits into the key hole (active site) of the lock (enzyme). Smaller keys,
larger keys, or incorrectly positioned teeth on keys (incorrectly shaped or sized substrate molecules)
do not fit into the lock (enzyme). Only the correctly shaped key opens a

Lab Report On The Effect Of Enzyme Concentration On...
In the first part of the lab, 5 solutions were tested for the Benedict's test along with Iodine test, what
was observed was the reaction rate vs. enzyme concentration. As shown on the plot #1 graph, the
concentration of the salivary amylase increases, the faster it turned into light brown, meaning the
faster it broke down into glucose subunits. Specifically, in test tube 11, it contained 2ml of 10%
salivary amylase and 2ml of the buffer, this solution turned into a light brown in 25 seconds. This
because when the concentration of the enzyme is higher, there are more active sites for the substrate
to bind to. Therefore, the enzyme is breaking down the substrate into smaller and smaller subunits of
glucose, causing it to have a negative result for the Iodine test along with having a positive result for
the Benedict's test due to there being more reducing sugars (Valls, Rojas, Pujadas, Garcia–Vallve, &
Mulero, 2012).Furthermore, in the test tube 12, it contained 5% of salivary amylase and 2ml of
buffer. The Iodine test for this solution turned into a light brown colour in 30 seconds because the
concentration of the enzyme was decreased, thus not having as many sites for the substrate to bind
to and break down the starch into glucose subunits. For the Benedict's test, the solution was broken
down into smaller subunits and causing it to have a positive result by turning into a light brown. The
tube containing 2% salivary amylase turned into a light brown colour for the Iodine

Amylase Lab Report
Abstract An experiment was performed to test how temperature variations affect enzymatic activity
of the enzyme amylase. The results of the experiment will also determine the optimal temperature of
the amylase enzyme. The results of the experiment provide evidence for determining the
environments that the enzyme amylase would most likely be present. By determining the possible
environments, one can predict what and how environmental factors will affect the enzyme amylase.
Two forms of amylase (Bacterial – Bacillus licheniformis and Fungal – Aspergyllus oryzae) were
combined with starch molecules at four different temperatures (0⁰, 25⁰, 65⁰, 85⁰ Celsius). The
combination of starch and the amylase enzyme resulted in a visual chemical reaction that was
recorded. The enzyme activity was recorded every two minutes, starting at 0 and ending at 10. The
start time 0 served as the control group of the experiment. The results concluded that both bacterial
and fungal amylase has an optimal temperature around 65⁰C. This was possible to determine by
recording the color change of the spot plate wells. Amylase catalyzes efficiently at its optimal
temperature which resulted in yellow spot plate wells. Enzymatic activity decreased when the
temperature was less than 65⁰C, resulting in a green–brown well. The green wells indicated that
starch wasn't broken down completely and was still present. Temperatures greater than 65⁰C resulted
dark–green wells which resembled the denaturing of

Rate Of Amylase Lab Report
Purpose of Investigation To study how pH and temperature would effect the reaction rate for
amylase on starch.
Amylase is an enzyme found in human saliva and pancreas. It is the digestive enzyme that is needed
to breakdown starch molecules. Amylase must be kept at certain conditions to function at its
optimum level. The efficiency of starch digestion by amylase can be measured by how much simple
sugar it produces under various conditions. This experiment will explore the effect of pH (3, 5, 9,
and 11) on the function of amylase by using starch.
Hypothesis
Amylase have an optimal temperature and pH at which it functions. Amylase works best at pHs of
body temperature in humans. If the pH deviates extremely in either direction (higher or lower) ...
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Factors that may cause the enzyme to denature are pH and temperature. When an enzyme is
denatured, it can no longer bind to the active site, and therefore cannot carry out its functions.
Therefore, adding pH buffer to amylase will affect the enzyme's function uopn its addition to starch.
Materials and Methods
Prepare 8 clean, dry test tubes in a stand and label them #1–8 with masking tape. Carefully and
generously spit into test tube 1–8 and add 2–3 ml of distilled water.
Effect of Temperature
1. Place test tube 1 into a room temperature bath, place test tube 2 into an ice water bath (0), place
test tube 3 into warm water bath (37) and place test tube 4 into a hot water bath (80).
2. Add 5ml of 1% starch solution into test tubes 1, 2, 3, and 4. Mix the starch solution with the saliva
thoroughly.
3. After 10 minutes, conduct the Benedict's test. Add 3 ml of Benedict's reagent and swirl the test
tubes gently to mix the contents. Place the test tubes into the hot water bath and record observations
after 5

Digestion of Starch by the Action of Salivary Amylase
Austin Peay State University Department of Chemistry
CHEM 1021
BREAKING DOWN STARCH USING SALIVARY AMYLASE Caution: You will be using a
Bunsen burner and glassware to create your own constant water bath. Appropriate caution should be
exercised when dealing with the Bunsen burner, hot water, and glassware. Purpose: Many plants
store their energy in the form of starch, a polysaccharide made from repeating units of the
monosaccharide glucose. Our bodies break down starch into the individual glucose units, which are
further metabolized into CO2 and water through the process of glycolysis–this is the process we
commonly call digestion. The enzyme amylase is present in our saliva and ... Show more content on
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Pour this into a clean 50‐mL beaker to mix. In a 100‐mL graduated cylinder, put in 1 mL of saliva
and 99 mL of water for the 1% solution. Pour this into a clean 150‐mL beaker to mix. 3. Set up 10
reaction tubes (label with a wax pencil) of varying saliva concentrations in a test tube rack as
follows: Tube # Saliva Distilled water Final saliva % 1 3 mL 100% 0 mL 100% 2 2 mL 100% 1 mL
66.7% 3 1 mL 100% 2 mL 33.3% 4 3 mL 10% 0 mL 10% 5 2 mL 10% 1 mL 6.7% 6 1 mL 10% 2
mL 3.3% 7 3 mL 1% 0 mL 1% 8 2 mL 1% 1 mL 0.67% 9 1 mL 1% 2 mL 0.33 % 10 0 mL 3 mL 0%
4. Start the reactions: Add 3 mL of a 2% starch solution to the tubes. Mix, and then simultaneously
add all 10 tubes to the water bath. After exactly 30 minutes, add 2 drops of the iodine solution to the
tubes and record the resultant color. A blue solution means starch still remains, and a colorless
solution means all starch has been broken down into glucose.
Revision SP11 Page 2 of 7
Austin Peay State University Department of Chemistry
CHEM 1021
BREAKING DOWN STARCH USING SALIVARY AMYLASE 5. Determine the amylase number:
a. Find the most dilute solution of saliva that

The Effect Of Enzyme Amylase On The Commercial World And It
The enzyme, Amylase is significant to the commercial world and it is important to know the optimal
conditions for amylase activity to be able to use amylase efficiently. To determine the optimal
temperature for both fungal and bacterial amylase, an Iodine test was used to visually measure
starch catalysis. A mixture of starch and amylase, either bacterial or fungal, were placed in four
different temperatures, 0⁰C, 25⁰C, 55⁰C, and 85⁰C, and then added to iodine to observe amylase
activity. A light yellow color means a weak presence of starch which indicates a high activity rate
for amylase while a dark blue–black color means a strong presence of starch which indicates a low
activity rate for amylase. Observed was an optimal temperature of 55⁰C for bacterial amylase which
showed the lightest yellow color and an optimal temperature around 25⁰C for fungal amylase which
showed the lightest yellow color.
Introduction
Enzymes are biological catalysts that regulate chemical reactions which accomplish a constant
production of energy that all biological processes require. These proteins are vital to maintaining
functionality in people's daily lives and the absence of an enzyme can cause detrimental harm in the
form of illness or even death (Alberte, Pitzer, Calero 49). Enzymes are also used commercially to
improve the standard of living. Amylase, for example, an enzyme that is used to break down protein
and starch: a storage polysaccharide, is among the most important that have been

The Effect Of Enzyme Concentration On The Rate Of Starch...
Monica Saripella
Beibei Xin: Thurs @ 5
2/19/14
Lab Report #1
The Effect of α–Amylase Concentration on the Rate of Starch Hydrolysis in a Porcine Pancreas
Introduction:
Our body uses various different types of molecules that work together in order to keep us
functioning. One of these molecules is called amylase. Amylase is an enzyme that breaks up the
glucose chains in starch into maltose. Enzymes work to speed up a reaction by lowering the
activation energy needed for the reaction to occur. There are three different types of amylase: α–
amylase, β–amylase, and γ–amylase. α–Amylase is commonly found in saliva and pancreas of many
animals. In this experiment, we used porcine pancreatic α–amylase in order to find the effect of
different factors on the rate of the digestion of starch. The activity of α–Amylase can be affected by
the concentration of amylase, the pH of the environment surrounding amylase, and the temperature
that the reaction using amylase occurs in. This indicates that a change in any of these factors can
affect the enzyme, increasing or decreasing the rate that the reaction occurs: in the case of amylase it
indicates the rate that starch is digested, or maltose is created. All enzymes, α–Amylase included,
operate best in an optimal range of pH, temperature, and concentration; at these optimal conditions
the reaction will occur in the fastest amount of time (Ceska et al., 1969). In particular, this report
will focus on the effects of enzyme

Biological Branches Of The Complex Study Of Life
ABSTRACT Throughout history, there have been many studies conducted regarding different
biological branches of the complex study of life. Amylase, an enzyme that catabolizes starch
polymers, is one of the most important enzymes needed for the production of certain foods, such as
syrups, and different processes such as fermentation. Like everything's biological nature, these
certain enzymes are affected by different factors ranging from pH levels to temperature. Finding out
the temperature at which these enzymes reach their optimal condition (conditions at which these
enzymes work the best), is one of the most revealing studies of all. In this experiment, the affect that
temperature has on the enzymatic activity of Amylase was the leading role, whether it was to
determine if it was slowing it down or speeding it up. For both experiments, iodine was used as the
control. First, the optimal temperatures of fungal Amylase were tested. For this particular task, there
was not too much changed noticed. For most of the temperatures, the activity change seen was very
minimal. With iodine and starch by itself, the activity remained the same as well as with the amylase
at the 85 degrees test. When testing for the bacterial Amylase, the most change was seen at the 55
degrees test. Overall, it can be said that as temperature rises or decreases, enzymatic activity is
affected, but of course with a certain plateau.
INTRODUCTION When it comes to

Literature Review On Saliva
Abstract: In the last 10 years, the use of saliva as a diagnostic fluid has become somewhat of a
translational research success story. Technologies are now available enabling saliva to be used to
diagnose disease and predict disease progression. This review describes some important recent
advances in salivary diagnostics and its application in various systemic diseases .This review will
also stimulate future research activity. Key word: saliva ,sjogren syndrome Introduction: Saliva is a
unique fluid and interest in it as a diagnostic medium has advanced exponentially in the last 10
years.The literature is replete with articles,2500+ since 1982, describing the use of saliva, gingival
crevicular fluid, and mucosal ... Show more content on Helpwriting.net ...
With the exception of sialometry (salivary flow rate determination), most salivary function tests
must be conducted in special laboratories or clinics. Included among these tests are sialography,
salivary scintigraphy, biopsies, and sero– logical tests. While these tests are helpful, they are
invasive, expensive, and not always conclusive (Daniels, 1996). Sreebny and Zhu (1996) proposed a
panel of salivary determinants that could be used clinically for the diagnosis of Sjogren's syndrome.
These include flow rate, pH, buffer capacity, lactobacillus, and yeast

Comparing Free to Immobilised Amylase Enzyme in Its...
Comparing Free to Immobilised Amylase Enzyme in Its Catalysis Rate
Method:
First of all, the Immobilised enzymes need to be made. The method used to create these immobilised
enzymes would be Micro encapsulation. This means that the enzyme used, in this experiment being
Amylase, is encapsulated inside Sodium alginate. The enzyme was believed to act quickly, so the
enzyme would have to be slightly diluted in order to get a good range of results. !0cm³ of Amylase
will be added to 20cm³ of Sodium alginate, and then mixed. Using a pipette, the Sodium Alginate –
Amylase mix is dropped into Calcium Chloride, and this will form the beads of Immobilised
enzymes needed for the experiment. As soon as ... Show more content on Helpwriting.net ...
The product made from adding Amylase and Starch together is Maltose, which is a Disaccharide, so
this is in essence, a reducing sugar test. Previous data from other experiments will be used to
compare methods in order to maximize the experiments efficiency.
In this experiment, there are many variables to consider. Temperature must be kept at a constant, and
at optimum for the Amylase, being at 35°c. Thermometers will be used to monitor the temperature
and a water bath will be used to heat the experiment. P.H. must also be kept at optimum and this will
be achieved by adding Buffer solution to the enzyme and substrate mix. The Buffer solution will
keep the mixture at p.H. 7.2, which again, is optimum for the Amylase. The overall volume of
enzyme and substrate must be kept the same, and hence concentrations must be kept the same too.
The overall volume will be 20cm³ and the concentrations will be kept the same. The independent
variable chosen is time. There will be different time periods that the enzyme and substrate are kept
together for both immobilised and free enzymes. There will be 30–second intervals between each
removal of the samples. Time is the independent variable because the catalysis rate is being
measured of immobilised enzymes and free enzymes, so time is the obvious choice. The rate of

The Effect Of Enzyme Enzymes On The Concentration Of An...
Introduction
Organisms cannot rely entirely on spontaneous reactions to produce all the materials necessary for
life. These reactions occur much too slowly. To produce these materials quicker, cells rely on
enzymes, biological catalysts, to speed up these reactions without being consumed. (General
Biology I, Martineau, Dean, Gilliland, & Soderstrom, Lab Manual, 2017, 43). To produce these
materials quicker, the activation reaction much be lowered, a very important part of this lab. Each
enzyme acts on a specific molecule, or set of molecules, called a substrate (43). The enzyme binds
to this substrate, forming an enzyme–substrate complex. An enzyme is a protein whose structure is
determined by the sequence of amino acids groups that ... Show more content on Helpwriting.net ...
Methods
Experiment 1: Constructing a Standard Curve
The students first prepared to construct a standard curve. To do this, each group measured the
absorbance of starch solutions of unknown concentrations treated with IKI (General Biology I,
Martineau, Dean, Gilliland, & Soderstrom, Lab Manual, 2017, 45). The absorbance values were
determined for a range of samples, and plotted on a graph. A line of best fit was then used as a
reference to determine the amount of starch present in unknown samples.
Using the yellow tube, which included everything but starch, as the blank, each group zeroed their
spectrophotometer. This was done so that any absorbance observed depends only on the amount of
starch present, not on any other reagents (buffer, IKI). To zero the spectrophotometer, the
wavelength was first set at 580nm, using knob 3 (45). Next, the groups made sure that the light next
to "transmittance" was lit, and the chamber to be tightly closed. Having the chamber empty & closed
tightly provides reference for the darkest condition possible. Using knob 1, the transmittance was
turned until it read 0.0 (45). Before the groups used their blank test tube to zero the
spectrophotometer, each needed to wipe the tube with kimwipes to ensure a clean reading. Turning
knob 2, each group was then instructed to zero the absorbance, 0.000. Upon removing the blank,
each trial was inserted into the chamber (46). The

Amylase Temperature Lab Report
The Effect of different Temperatures on the reaction rate of Amylase Introduction: Amylases are
enzymes that breaks down starch which accelerates the hydrolysis of glycosidic bonds in
polysaccharides (S. Sivaramakrishnan et al., 2006). They bond with certain substrates to effectively
increase the reaction rate of a chemical experiment. Most enzymes are very specific, as in they
would only bond with a distinct substrate for it to cause a certain reaction. This can be described
with the key and lock analogy. Only one type of key, certain amylase, will be able to open a
particular lock, substrate. Without amylase, a lot of the organs necessary for people will no longer be
able to react as fast, like the digestion of food or respiration. It speeds ... Show more content on
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T., Vogelsong, K. M., Lu, Y., Ellman, A. B., & Hudgens, G. A. (1996). Salivary α–amylase as a
measure of endogenous adrenergic activity. Clin Physiol Clinical Physiology, 16(4), 433–448.
Hiromi, K., Takasaki, Y., & Ono, S. (1963). Kinetics of Hydrolytic Reaction Catalyzed by
Crystalline Bacterial α–Amylase. III. The Influence of Temperature. Bulletin of the Chemical
Society of Japan Bull. Chem. Soc. Jpn., 36(5), 563–569. Malhotra, R., Noorwez, S., &
Satyanarayana, T. (2000). Production and partial characterization of thermostable and calcium–
independent alpha–amylase of an extreme thermophile Bacillus thermooleovorans NP54. Letters in
Applied Microbiology Lett Appl Microbiol, 31(5), 378–384. Sivaramakrishnan, S. (march 11.2006).
͢ᾀ– Amylases from Microbial Sources– An Overview on Recent Developments. Food Technology
Biotechnology, 44(2), 173–184. Sudhan, H., & Priya, S. (2012). Isolation and Production
Optimization of Amylase Producing Bacteria from Soil by Submerged Culture Method. Research
Gate: Pharmaceutical Sciences, 1(2012), 8–10. Retrieved February 17,

The Effect Of Temperature And Ph Of Enzymes Activity...
The effects on temperature and ph of enzymes activity saliva amylase
Term 3
Year level; Twelve
Name; Michelle Van Biljon
Teacher; Miss
Draft due; Week 5 (Tuesday)
Due date; Week 6 (Tuesday)
Introduction
The enzymes inside the human body is a protein molecule which is a biological catalyst containing 3
types of characteristics. The first characteristic of an enzyme is to increase inside the human body
depending on the rate of reaction. Secondly most of the enzymes inside the human body will take
control and only act specifically upon one reactant, this is called the substrate, and this is the
enzyme that produces products. Third most important is the enzymes strongly regulate in a circle,
from a low concentration (activity) to a high concentration (activity) then back around vice versa.
The enzymes can strongly be affected in the changes of both the temperature and the different ph
levels. Every individual enzyme works to a certain extent reacting to a certain ph level and
temperature, its activity decreasing at values above and below that point due to denaturation. For
enzymes, denaturation can be defined as the loss of enough structure rendering the enzyme inactive.
The tertiary structure of the enzymes and their function also includes the non covalent force in
creating and determining the shape and the structure of all enzymes. The salivary amylase is found
in the salivary glands inside the human body which is produced by the ptyalin. Maltose and
Isomaltose are a

Does Amylase Affect The Rate Of Enzyme Activity
Introduction: Enzymes are biological catalysts that lower the activation energy required for a
reaction to take place. They speeds up the process of the reaction, while still not being consumed,
they can function multiple times. Enzymes are specific to molecules or sets of molecules and only
work with these specific substrates. The enzymes cause substrates to be converted to products faster
than they would without enzymes. A substrate fits into an enzyme, which then catalyzes the
conversion of the substrate into products. The enzyme facilitates reactions, however it can become
denatured. When an enzyme is denatured its form changes, thus preventing its function of
converting substrates to products faster, and the enzyme does not work. The enzyme used in this
experiment is amylase. Amylase is an enzyme that catalyzes the breakdown of the polysaccharide
starch into the disaccharide maltose. Amylase is produced by human salivary glands and aids in
digestion and breaking down food substances. ... Show more content on Helpwriting.net ...
The biological hypothesis is, temperature has an effect on the rate of starch digestion by the
amylase. The null hypothesis is, there is no significant change in amylase activity as the temperature
changes. Any deviations observed is due to chance. The alternative hypothesis is, there is a
significant change in amylase activity as the temperature changes and the temperature has
significant effect on amylase activity. The prediction is that temperature has a significant effect on
amylase activity and the null hypothesis will be rejected. This will be indicated by tube 2 showing
the most starch digested, which would be caused by the most enzyme

Fungal Amylase Lab Report
Finding the optimal temperature for enzymatic activity of bacterial and fungal amylase was the main
purpose of the experiment. The effectiveness of an enzyme can be affected by the environment of
the organism is in, and to work at its best, the optimal temperature is necessary to breakdown
nutrients and produce energy. The results for this particular experiment showed that the optimal
temperature for both amylases was 65°C. This is because at this temperature, the breakdown of
starch was the most effective, being able to catabolize the starch into minor subunits like maltose
(which organisms can then use as energy storage and as a source of food) (Alberte et al., 2012). In a
low temperature such as 0°C, neither of the amylases was able to hydrolyze starch and this is
because this temperature is way below the optimal temperature, very little enzymatic activity can
happen since substrate molecules have less energy to bind into the active site and so slower (Ibrahim
et al., 2012). ... Show more content on Helpwriting.net ...
This leads to denaturation of the enzyme in which the active site of the enzyme changes shape with
elevated temperatures and decreases the possibility of substrate binding (Alberte et al., 2012).
Furthermore, the real optimal temperature or time where 100% hydrolysis occurred for fungal
amylase was not found since there was very little change in enzyme activity at the optimal
temperatures as time progressed during the 10 minutes of the trial. This states that the experiment
may need to be repeated over a lengthier period of time. As seen in Graph 1 and 2, as time
progressed, hydrolysis increased in certain temperatures for both fungal and bacterial amylases, and
in some temperatures, hydrolysis was consistent with little or no

The Effects of Enzyme Concentration on the Activity of...
The Effects of Enzyme Concentration on the Activity of Amylase
To investigate the effect of Amylase concentration on its activity. the relative activity of Amylase is
found by noting the time taken for the starch substrate to be broken down, that is, when it is no
longer gives a blue–black colour when tested with iodine solution. This time is referred to as the
achromatic point.
Equipment:
v Amylase solution 0.1%
v Starch Solution 1.0%
v Distilled water
v Iodine in potassium iodine solution
v White tile and polythene pipette
v Graduate pipettes or syringes
v Test tubes in rack
v Beaker (used as water bath)
v Stopwatch, Thermometer
v Eye Protection ... Show more content on Helpwriting.net ...
Its function is to catalyse the hydrolysis of amylose and amylopectin to a mixture of products,
including maltose and dextrin, which are polysaccharides. Maltose consists of two alpha glucose
remains joined by 1,4 linkage; Dextrin is made up of several alpha glucose units joined by 1,4 and
1,6 linkages. Pullulanase, also known as debranching enzyme, hydrolysis the alpha 1,6 links at the
branching points in the polysaccharide. Commercial sources of these enzymes include bacteria and
fungi. Fungi amylases are used to clarify fruits juices, wines and beer by removing suspended
starch. In bread making for example addition of amylases can yield more sugars from the starch in

flour and barley grains, another commercial which is statue of import ants is the conversion of
starch to sweet glucose syrups which are used generally as sweeteners in food industry as well as in
the bread–making and brewing industry. Altering the balance between amyloglucosidase and the
fungi alpha amylase can produce different proportions of glucose and maltose. A higher proportion
of glucose is useful for fermentation whereas higher maltose is more useful in preparation of jam
and confectionary. The Amylase Enzyme breaks down starch; which is a carbohydrate.
Results Table:
Amylase Concentration
Time Taken to reach Achromatic Point
Pure Water (control) 0%
Didn't do any

Environmental Factors Influencing Amylase Enzyme Activity
Abstract: Enzymes are specific–type proteins that act as a catalyst by lowering the activation energy
of a reaction. Each enzyme binds closely to the substrate; this greatly increases the reaction rate of
the bounded substrate. Amylase enzyme, just like any other enzyme, has an optimum PH and
temperature range in which it is most active, and in which the substrate binds most easily. The
purpose of this experiment was to determine (1) the reaction rate of an amylase enzyme in starch
and (2) the environmental factors that can affect the enzymatic activity. The hypothesis, in relation
to the enzymatic activity by variables such as the substrate concentrations, temperature, PH and
chemical interactions on the rate of reaction, stated ... Show more content on Helpwriting.net ...
The optimal temperature permits the utmost number of molecular collisions and the fastest alteration
of the reactants to product molecules. Most human enzymes have an optimal temperature of about
35–40°C (close to body temperature 37°C). In addition to an optimal temperature, every enzyme
also has optimal PH values at which it is the most active. The optimal PH value for most enzymes
fall in the range of PH 6–8 (close to neutral PH 7); however some digestive enzymes in the human
stomach work best at very acidic PH of 2. In this lab experiment the action of the enzyme Amylase
was observed on starch (the substrate). Amylase changed the starch into a simpler form, the sugar
maltose, which is soluble in water. Maltose then breaks down the glucose chains of starch in the
pancreas and intestines. Amylase is present in human saliva, and begins to act on the starch in the
food while still in the mouth. Exposure to heat or extreme PH (acid or base) will denature proteins.
Enzymes, including amylase, are proteins; if denatured enzymes can no longer act as a catalyst for
the reaction. In the presence of potassium iodide, starch turns a dark purple color; however maltose
does not react with I2KI. The rate of fading of starch allows a quantitative measurement of reaction
rate. Enzymes have an ideal range of values for any of the variables, or optimal conditions, in this
experiment. When these optimal conditions are

What Is The Effect Of Ph On The Activity Of The Enzyme...
The Effect of pH on the Activity of the Enzyme Amylase
Aim :–
To find the effect of pH on the activity of the enzyme amylase.
An enzyme is a type of protein found in all living cells. Enzymes act as biological catalysts,
breaking down substrates without needing a high temperature, allowing all the chemical reactions of
metabolism to take place, regulating the speed at which they progress, lowering the activation
energy and providing a means of controlling individual biochemical pathways.
Enzymes owe their activity to the precise three–dimensional shape of their molecules. According to
the 'lock–and–key' hypothesis, the substrates upon which an enzyme fit into a special slot in the
enzyme ... Show more content on Helpwriting.net ...
The acidity of a chemical is determined by how concentrated the chemical is with Hydrogen ions.
This is describe in an example
Loses H Gains H
Alkaline solution Acidic Solution
NH CHRCOO ç NH CHRCOO è NH CHRCOOH
Overall Negative charge "Zwitterion" Overall Positive charge
lost H so makes solution No change gained H so makes solution
more acidic. less acidic.
As the solution becomes more concentrated with hydrogen ions the more effective it is on taking up
the R (residual) group on amino acids: Lys, Arg, His, Asp and Glu. This affects the way in which
they bond with each other therefore affect their 3D arrangement. So if the ionic bonds are important
to structural stability, then the shape of the enzyme will change which in turn affects the
functionality of the enzyme.

As a type of protein, enzymes are easily affected by changes in pH. At their optimum pH the shape
of the enzyme is such the active site can fit perfectly with the substrate. As the pH deviates, either
decrease or increase from the optimum the acid or base conditions begin to disrupt some of the
loops between the loops of the protein chains. If this disruption occurs on the active site the site will
become distorted and the substrate will not fit perfectly. Thus not all enzymes will be able to
catalyse (break down) their reaction. Further increase or

Ph Buffers To Amylase On The Rate Of Starch

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Ph Buffers To Amylase On The Rate Of Starch