Design Experiment

Design Experiment
Design Experiment: Enzyme Inhibitors.
Research question: What is the effect of adding lead nitrate solution on the activity of amylase enzyme?
Aim: To test the effect of adding nitrate solution on the activity of amylase.
Background Information:
Inhibitors are molecules which repress or prevent another molecule from engaging in a reaction. They are substances that attach themselves onto an
enzyme and reduce or prevent the enzyme's ability to catalyse reactions. Competitive Inhibitors are inhibitors that occupy the active site of an enzyme
or the binding Site of a receptor and prevent the normal substrate or ligand from binding. An active site is a region on the surface of an enzyme to
which substrates bind and which catalyzes a chemical ... Show more content on Helpwriting.net ...
This is because a greater mass of lead nitrate reduces the ability of the amylase to breakdown starch into maltose. Therefore lead nitrate acts as a
non–competitive inhibitor reducing the enzyme's ability to catalyse the reaction. Lead nitrate is non–competitive because it affects the enzyme's
activity even though it is present in small quantities. The hypothesis were proven since the lead nitrate changes the shape of the active site of the
enzyme and prevents some starch molecules from binding to the active site for catalysts. According to the results obtained from the experiment, my
hypothesis is accepted and is correct. My hypothesis was, "There is an inverse relationship between the mass of lead nitrate and the ability of amylase
to convert starch into maltose." Despite the results obtained were correct and proved that the experiment was a success a few variables emerged during
the performance of the experiment that if improved could result to a more accurate result. We didn't have enough time to do this experiment over and
over again so we didn't have enough results to compare. Another important factor that may have influenced in our experiment was the quantity taken of
the lead nitrate. We didn't have any colorimeter so our result might not be
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How Does Substrate Concentration Affect The Rate Of Enzymes
Enzymes are globular proteins that act as catalysts which affect the rate of chemical reaction without being destroyed or altered during the process.
They are very effective in the body systems of organisms, an enzyme that catalyzes more than one thousand chemical reactions per second. But there
are certain conditions that enzymes can work normally or efficiently, such as the temperature of the environment must be correct for each enzyme
because different enzymes will have different optimum temperature ranges in which they can live; pH levels in the environment must also be correct
because if the environment around the enzyme is too basic or acidic, the enzyme will quickly denature; substrate concentration also affects the rate of
reaction ... Show more content on Helpwriting.net ...
Enzymes are organic catalysts and can speed up chemical reactions. Two molecules of hydrogen peroxide are broken down into two molecules of
water and a molecule of oxygen gas. Both water and oxygen are harmless to cells and therefore, the presence of catalase allows cells to break down the
toxic substance hydrogen peroxide before cells become poisoned.
The mechanism is that the enzyme bind to the substrate at the active site. The combination is called the enzyme/substrate complex. Enzymes only
work with specific molecules. The active site is a specially shaped area of the enzyme that fits around the substrate. Catalysis is when the substrate is
changed. It can be broken down or combined with another molecule to make a new one by breaking or building bonds. Then the enzyme/product
complex is produced. When the enzyme is released, it goes back to its original shape and repeats the process.
The enzyme in plants or human body is the most active at room temperature, because it has to achieve the highest efficiency. Therefore, when
conditions change, such as increasing or decreasing the temperature of the reaction, the enzyme activity will be inhibited and less efficient. This can
lead to the decomposition of hydrogen peroxide, which is not efficient, and can be toxic in organs.

The Effect Of Enzyme And Substrate On Chemical Reaction...
Abstract In this experiment we tested the effects that enzymes and substrate have on chemical reaction rates, which is the rate at which chemical
reactions occur.. This experiment tested how different concentrations of enzyme and substrate affected the light absorption measurements on a
spectrophotometer. The experiment also tested how temperature affected the light absorption, and in a separate test, the effect of the enzyme inhibitor
hydroxylamine was also tested. In the first test conducted, 3 different concentrations of enzyme, and three different concentrations of substrate were
measured in a spectrophotometer. For the enzyme and the substrate, the measurements got higher as the concentrations were higher, but the over
measurements of the substrate were smaller than those of the enzyme. In the second test conducted, the medium concentration enzyme was tested
under the temperatures; 4В°C, 23В°C, 37В°C, and 60В°C. The measurements in this test got higher as the temperature got higher, but did the
measurements under 4В°C were overall significantly higher than the other temperature measurements. Lastly, the last test conducted showed that the
measurements of the substance with 0 and 1 drop of hydroxylamine inhibitor went up, but the measurements of the enzyme with 5 drops of
hydroxylamine inhibitor stayed rather low and did not change much. In conclusion, these experiments showed that chemical reaction rates are sped up
with higher concentrations of enzyme, substrate,

Essay On Substrate Specificity Of Enzymes
Substrate Specificity of Enzymes
A substrate is a substance that the enzyme acts on. When an enzyme binds to its substrate at the active site of the enzyme, an enzyme–substrate
complex is created. While in the complex, chemical reactions takes place and products are made.
Enzymes have specific shapes that determine their functions.
The shapes accommodate very specific molecules.
Enzymes change shape after chemical reactions. There different energy changes with the reactions due to the state of the enzyme.
The active site also changes shape when the substrate binds to it, thus allows for the site to have an induced fit.
Catalysis in the Enzyme's Active Site
In the active site of the enzyme, the substrate bonds with weak bonds such as ... Show more content on Helpwriting.net ...
The normal temperature for enzymes is between 35 and 40 degrees celsius.
Most enzymes function at around a 6–7 pH levels.
Some enzymes such as pepsin, which is an acid in the stomach, is activated at a pH of 2.
Cofactors
Cofactors such as ions and metals are nonprotein helpers to enzymes.
A cofactor that is an enzyme is known as a coenzyme.
Enzyme Inhibitors
Competitive inhibitors are inhibitors that block substrates from binding to the active sites of enzymes.
They make the enzyme less effective.
Noncompetitive inhibitors are inhibitors that bind to the outside of an enzyme far away from the active, to change its shape and reduce its effectiveness.
If inhibitors bond covalently to the enzyme, then the inhibitors are permanent.
For example, in poisons such as DDT, antibiotics also use such inhibitors to kill bacteria.
Although it is used to regulate cellular enzymatic activity, inhibition is harmful.
The Evolution of Enzymes

The function and diversity of enzymes is due to gene mutations. If a gene of an enzyme changes, the protein will have one or more different amino
acids which can impact an enzyme's activity or allow it to bind to different substrates.
Enzyme – A protein
Catalyst – Speeds up chemical reactions.
Activation Energy – Energy required to produce a chemical reaction.
Substrate – The reactant.
Enzyme/Substrate Complex – A substrate's interaction with an enzyme.
Active Site – The site of an

The Effect Of Enzymes On Enzyme And Substrate
Introduction:
Enzymes defined as biological catalysts that speed the chemical reaction by reducing the activation energy (Biology Department, 2014). Enzymes play
an important biological role in the cell, as it is important to keep the cell alive by speed up the reaction, which explains why in absence of enzyme some
reactions need long time (Richard & Mark, 2001). Also, enzymes regulate organism intercellular function for example enzymes help to keep human
body healthy by defend it from infection, regulate blood sugar, and maintenance weight (Reece et al., 2014). Reaction rate can be affected by pH,
temperature, and concentration of enzyme and substrate (Biology Department, 2014). If pH levels are not in the enzyme normal range the active site
of the enzymes will change its shape so the enzyme will not be able to combine with the substrates, which will prohibit the converting of the substrate
to product (Reece et al., 2014). Temperature effect the molecules movement for enzyme and substrate in the solution so if the temperature increase the
molecules movement will increase and this will increase the rate of reaction until the point that the energy became so high this will prohibit substrate
from binding due to the fact that the active site of the enzyme were altered (Biology Department, 2014). If enzymes concentration increase the amount
of product per unit time will increase too, while the total amount of product will not change (Richard & Mark, 2001). It is important

Enzyme Kinetics of Beta-Galactosidase
Abstract
This experiment is to study and measure the enzyme activity of ОІ–galactosidase in the different concentrations of o–Nitrophenylgalactoside (ONPG)
using a spectrophotometer. The spectrophotometer was also set at 420nm, a wavelength which is best for recording the absorbance values for the
experiment. From the results, 0.9mM ONPG solution has the highest absorbance and 0.1mM ONPG solution has the least. Also, 0.5mM ONPG
solution has the highest rate of enzyme activity and it is the most efficient as the enzyme activity of the ONPG solution continues even though the other
concentrations of ONPG solution has already stopped the enzymatic reactions as the substrate is already used up.
Introduction
This experiment is to study and ... Show more content on Helpwriting.net ...
However, the rate of reaction only increases for a certain period of time until there is lesser substrate molecules than the enzyme molecules. The
increase of enzyme concentration does not have effect if there are lesser substrate molecules than enzyme molecules initially.
A spectrophotometer is an instrument which measures the amount of light of a specified wavelength which passes through a medium. This instrument
is usually used for the measurement of reflectance of solutions. Light is separate into different wavelengths and is being passed through the sample
solution. The sample solution will have its own wavelength and will absorb a certain amount of light. The higher the molecular concentration, the
higher the absorbance value.
Materials and methods
Materials needed for Experiment 6:
Samples: 0.1mM, 0.5mM, 0.7mM, 0.9mM and 1.0mM o–Nitrophenylgalactoside (ONPG) solutions
Reagents: Grade 6 ОІ–galactosidase (SIGMA), sodium phosphate buffer pH 7.3
Apparatus: Spectrophotometer (UV–1201), cuvettes, water bath (set at 37В°C), 200Вµl and 1000Вµl micropipettes and test tube
Methods for Experiment 6: 1. 5 different concentrations of ONPG solutions was provided. 2. The different concentrations of ONPG solutions and
buffer solutions were incubated in the water bath at 37В°C for 5 minutes. 3. The spectrophotometer was set at 420nm. Distilled water was also used as
the 'blank'. 4. 200Вµl of ONPG solutions, which is the

Investigating The Levels Of Substrate Concentration And Ph...
Enzymes are one of an important function to the body. An enzyme is a catalyst that speeds up chemical reactions without being used up in the process
(Leady 2017). In simpler terms, it is a substance that is used for chemical reactions to accelerate the chemical reaction, and create a new product from
the previous substance without changing the chemical compounds. Not all of the enzymes work the same. Some of the enzymes can either be affected
by a different pH, or a different substrate concentration. When conducting experiments, the pH, or the substrates have to be similar because if the
products are in a different area, then the results will be completely different. This is why experiments conducted have to have a similar area. The
experiment conducted is about the different levels of concentration. The question is will different levels of substrate concentration and pH affect enzyme
function? The hypothesis is that the pH with a higher pH will effect it more, and a substrate concentration with a higher substrate concentration will
have a higher effect. The prediction points to the area of the pH9 having the greatest effect out of the 4 groups, and a 12% H2O2 concentration also
having the greatest effect out of the 4 groups.
Methods: The method I used in the experiment was followed by the lab manual of "Fundamentals of Life Science by Brenda Leady" (Leady 2017).
We conducted an experiment of 8 different tests, 4 of the different classifications of pH, and 4 different

Enzyme Activity Lab Report
Discussion:
The results of the three–part experiment provide a deeper knowledge about the factors that influence the rate of the reaction of the enzyme activity and
how the factors influence the structure or function of the enzyme. After conducting the experiment in Part A, the results were the same as the
hypothesis that as the number of disks increases the enzyme activity also, proportionally increase simultaneously shown clearly in figure achieved.
When three disks were utilized, increasing the enzyme concentration enabling the molecules to collide with more hydrogen peroxide substrate
molecules decomposing at a faster rate enabling more product to be formed. It can be seen that the Vmax approximately occurs at 230 kpa, indicating
that ... Show more content on Helpwriting.net ...
All hypotheses predicted were correct for all factors tested according to the appropriate justification, except for one hypothesis in Part C. In Part A
the increased number of enzyme concentration (also known as beef liver catalase) increases the rate of the reaction increases as well so long as all
other factors such as pH, ionic concentrations and temperature remain unchanged or fixed. Furthermore, if diluted concentrations of 1.5 % and 3% the
substrate concentration increases and the rate of the reaction until it reaches a limiting factor and becomes fully saturated. However, if simply
distilled water without hydrogen peroxide is utilized the hydrogen peroxide would decrease as the rate of the reaction because no substrate enzyme
complex will be formed therefore creating no products. Lastly, increasing the concentration of heavy metal ions, such as copper (II) Sulphate and lead
(II) nitrate, will decrease the rate of the reaction as it will disrupt the bonds between the amino acids of the proteins denaturing the enzyme structure
and function. It was learned that if distilled water is used without the concentrations of copper(II) Sulphate and lead (II) nitrate the rate of the reaction
decreased as the heavy metal salts decreased. As a result of more water molecules, there is no substrate or enzyme catalase the reaction and quickly
form a

Michaelis-Menten Kinetics
Introduction:
Enzymes are biological macromolecule that acts as catalyst and speed up reaction by lowering the activation energy of the chemical reaction without
altering the thermodynamic of reaction (study.com). However, the enzymes are not consumed in the reaction and they will regenerate (study.com).
According to rsc.org, enzymes have an active site. The reacting molecule that binds to enzyme is called the substrate (rsc.org). Enzymes catalyze
reactions by interacting with the substrate and the subsequent transition state. These interactions release energy and therefore stabilize the transition
state, which ultimately lowers the activation energy of the reaction (rsc.org).
The purpose of this lab is to measure how an enzyme responds to the presence of an inhibitor in various concentrations, and identify what type of
inhibitor that involved. In this lab, we used the Michaelis– Menten Kinetic, which proposed by two scientists Leonor Michael and Maud Leonora
Menten for enzymatic dynamics. The model explains how reaction rate depends on the concentration of substrate and enzyme (chemwiki.ucdavis.edu).
In the reaction of an enzyme catalyzed, the enzyme interacts with the substrate by binding to its active site to form the enzyme–substrate complex, ES.
The reaction is ... Show more content on Helpwriting.net ...
Km is the Michaelis constant. It is the substrate concentration at which the reaction velocity is half of the Vmax. [S] is the concentration of the
substrate (Washington.edu). From the Michaelis Menten Kinetic equation, we have many different ways to find Km and Vmax such as
Lineweaver–Burk plot, Hanes–Woolf plot, etc. However, this lab used the Lineweaver– Burk plot. By taking the reciprocal of the Michaelis Menten
Kinetics equation, we can obtain the Lineweaver –Burk double reciprocal plot, which is a linear line (chemwiki.ucdavis.edu). This provides more
precise way to determine Vmax and

Enzyme Peroxidase Lab
The purpose of this experiment is to see how the enzyme peroxidase performs under different conditions. An enzyme is a protein molecule that is a
biological catalyst. A catalyst is a substance that speeds up a chemical reaction, while also lowering the activation energy of a reaction. The activation
energy of a reaction is the initial amount of energy that is necessary to bring reactants together with the proper amount of energy and placement so that
products can be formed. Enzymes have a unique 3–D shape, which enables it to stabilize a temporary association between substrates (the reactant
molecules that binds to the active site of an enzyme and undergoes chemical modification). Most enzymes have pockets on their surface called active
sites. ... Show more content on Helpwriting.net ...
Given the right conditions to function, the enzyme can react with other molecules for as long as is needed. The substrate in this lab is H202, also
known as hydrogen peroxide. When hydrogen peroxide and peroxidase meet under the correct conditions they combine to form an enzyme–substrate
complex. During this reaction H202 is reduced to water, while guiaiacol combines with oxygen–producing tetra guiaiacol. Because tetraguiaiacol
creates a brown color the reaction rate can be measured by a Spectrophotometer. The Spectrophotometer measures the amount of light that passes
through a solution and then indicates the amount of light absorbed in comparison to the amount of light absorbed by a clear solution. The darker the
solution becomes, the greater the light absorbance is. Therefore, as the oxidized guiaiacol produces a brown color, the darker color causes the
spectrophotometer to absorb more light. The rate of which light absorbance increases is an indirect measurement of the rate of reaction in the solution.
Several conditions will be placed on the original substrates in order to determine the optimum conditions for this reaction to

The Effect Of Enzymes On The Enzymes
Background:
Enzymes are proteins with specific 3D conformations, or shapes, which allow them to interact with specifically shaped substrates in an active site
region. The function of enzymes is to speed up, or catalyze, reactions by lowering the activation energy (EA). The two types of enzymes are catabolic
and anabolic; the former assists in breaking down substrate, while the latter assists in building up, or combining, substrates.
At the molecular level, substrates must collide with enzymes with enough energy, at a specifically shaped active site, in order for enzymes assist in
turning substrate into product. An enzyme, with a specific structure that determines its function, has a selective active site, in which only certain ...
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Therefore, as time progresses and later into the trial, enzyme speed slows down, as more substrates have been turned into products. This was
demonstrated in the toothpickase lab, in which the graph showed the derivative/slope of the broken down substrate molecules originally increasing and
then decreasing as time progressed. In conclusion, the amount of enzyme stayed constant, and the amount of substrate decreased, while the amount of
product increased.
Methods: Materials and Procedures Materials:
– Turnip peroxidase (4%)
– 0.1% hydrogen peroxide
– 0.3% guaiacol
– Distilled Water
– 12 test tubes and a test tube rack
– Timer
– 1,5, and 10 mL syringes
– 6 Cuvettes (approx. 16x150 mm)
– Test tube cleaning sheet
– pH 3,5,6,7,8 and 10
– Spectrophotometer
– Funnel
–Safety goggles

(Safety precautions are listed in the procedures.)
Procedure 1:
Step 1–Make a blank using 13.3 mL of distilled water, .2 mL of guaiacol, and 1.5 mL of enzyme extract. Then pour the blank into a cuvette and clean
the edges with a cleaning sheet and insert into spectrophotometer. Press the calibration button and then wait until it is at zero absorbance.
Step 2– Mark one test tube substrate and another enzyme. Mix 7 mL distilled water, 0.3 mL hydrogen peroxide, and 0.2 mL guaiacol into the
substrate tube. Then mix 6 mL distilled water and 1.5 mL of peroxidase and add to the substrate

Why Are Enzymes Important?
Enzymes play a major part to human well– being. Some of their roles that they play in are digestion and nutrient assimilation, in immune response,
cognitive acceleration and cellular detoxification, among other things. Their main job is to accomplish specific functions throughout the body. The
pancreas is what produces most of the digestive enzymes which are then called pancreatic enzymes. Another thing that enzymes are important for
would be breaking down carbohydrates, protein, and fatty acids and preparing them for digestion. Substrates are molecules that enzymes help to bring
together. When substrates are brought together, the chance of achemical reaction occurring becomes higher and higher. Enzymes also lower the
activation energy of chemical ... Show more content on Helpwriting.net ...
The enzymes involved in respiration, photosynthesis and protein synthesis work inside the cells. Other enzymes are produced by specialized cells and
released from them. In the article paper by Dr. David Jockers, it lists some key enzymes for improving digestion. They include lactose, maltose,
amylase, cellulose, glucoamylase, alphagalactosidase and sucrose. These specific enzymes help reduce inflammation in the gut. The paper also
mentions proteolytic enzymes, also called protease, proteinase, or peptidase. They are necessary to metabolize protein molecules into amino acids.
They break the long chainlike molecules of proteins into shorter fragments and eventually into their components, amino acids. The article also mentions
symptoms of low pancreatic enzymes. Here are the following: bloating and cramping, diarrhea and constipation, flatulence (gas), low energy, fatigue
after meals, weight gain, food sensitivities, food in stools, and nutrient deficiencies. Another important thing that Dr. David mentions is that improper
digestion causes stress and inflammation in the gut lining that leads to complications of leaky gut

An Investigation on the Rate of Reaction of the Enzyme...
An Investigation on the rate of reaction of the enzyme Catalase on the substrate Hydrogen peroxide.
Plan
Aim: To investigate the rate of the effect of Catalase on hydrogen peroxide.
Introduction This investigation will be carried out to investigate the rate of reaction of the enzyme catalase on the substrate hydrogen peroxide.
Enzymes are biological catalysts, which speed up the rate of reaction without being used up during the reaction, which take place in living organisms.
They do this by lowering the activation energy. The activation energy is the energy needed to start the reaction.
Enzymes are essentially proteins and will only act in an aqueous environment. An enzyme is specific for a certain reaction or ... Show more content on
Helpwriting.net ...
This would be a suitable independent variable as it would be easy to change ourselves. If the concentration of the substrate increases the faster the
rate of reaction, as more hydrogen peroxide molecules can collide with catalase molecules, so more reactions will take place. As you increase the
concentration of substrate this will continue to occur up to a point where all the active sites on the enzyme are being used. The diagram above shows
the theory that the rate of reaction will continue to climb until all the active sites are being used and the rate will level off but does not stop.
S.A of the potato
Using different sizes of potato could show us whether the concentration of enzyme affect the rate of reaction. However, this would not be a
practical independent variable as the S.A to volume ratio would not be proportional and the size of the potato to get significant results would be
very hard to change. It would be very hard to cut the potato tubers to exact measurements and that could lead to the results becoming inaccurate. An
option could be to cut the potato tube into small 1 cm bits and pile then up on top of each other in the test tube, but this again would prove to be
impractical as then not all of the surface area of the potato would be exposed to the substrate and this would make my results unreliable. It may also
prove to be impractical as having the tuber bits piled on top of each

Effects Of Concentration On The Rate Of Reaction
Michaelis – Menten and Lineweaver – Burke kinetics of polyphenol oxidase . Effect of substrate concentration concentration on the rate of reaction"
Introduction
Enzymes catalyse biological reactions ,increasing the rate of chemical reactions
Enzymes have an affect on the structure of chemical transformation (stryer et al , 2011 )
Enzyme substances bind at the active cite which contains amino acid chains.
Without catalysis reactions the process would take place slowly to produce products , enzymes are most effective catalyst (Campbell and Farrell, 2011)
.A catalysed reaction is obtained by the production of a complex between e and the reactants (Montgomery et al ., 1990).The reversible reaction can be
seen below: E + S в‡„ ES в‡„ EP в‡„ E + P
Inhibitors
Competitive inhibitors bind to the active site of the enzyme and compete with substrate concentration. Competitive inhibitors do not change the vmax
velocity because high amounts of substrate can over come competitive inhibitors but rather increase km.
Non – competitive inhibitors cause blockage for enzymatic reactions but allow substrate to bind. Uncompetitive inhibitors don't bind to free energy but
rather to enzyme substrate concentration. Un– competitive inhibitors work more effective with high amounts of substrate concentration (Meisenberg
and Simmons , 2011).
Cofactors and Coenzyme
Non protein molecules are required by certain enzymes in order to participate in enzyme catalysed reactions (Devlin, 2010). Co factors are

The Effect Of Temperature On Enzyme Concentrations And...
The Effects of Varied Temperatures, pH Values, Enzyme Concentrations, and Substrate Concentrations on the Enzymatic Activity of Catecholase
By: Danielle Pasteur
October 12, 2015
BY 123L: 11:15–2:05
Introduction
An enzyme
Hypothesis
The null hypothesis will be that the test tubes with an increase in temperature, pH values, enzyme concentrations, and substrate concentration will have
a very small color change or no color change at all. The alternate hypothesis is that the test tubes containing an increase in temperature, pH values,
enzyme concentrations, and substrate concentration will all have an intense color change; the more the change, the more intense the color change will
be.
Material and Methods
The use of multiple test tubes and Parafilm was used for each experiment. Catechol, potato juice, pH 7 phosphate buffer, and stock potato extract 1:1
will be used to conduct the following experiments: temperature effect on enzyme activity, the effect of pH on enzyme action, the effect of enzyme
concentration, and the effect of substrate concentration on enzyme activity. For the temperature effect on enzyme activity, three test tube were filled
with three ml of pH 7 phosphate buffer and each test tube was labels 1.5 degrees Celsius, 20 В°C, and 60 В°C. The first test tube was placed in an
ice–water bath, the second test tube was left at room temperature, and the third test tube was placed in approximately 60В°C of warm water. After
filling the test tubes with three ml of the

Enzyme And Substrate Concentration Lab Report
BIOL 1406 Laboratory
Lilia Murray
October 3, 2015
The Effects of Enzyme and Substrate Concentrations in Various Factors
Abstract:
The entirety of this performed lab experiment is to test the effects of enzyme and substrate concentrations in varying factors such as reaction rate,
temperature, and the inhibitor hydroxlamine. What was first tested was the effect of substrate and enzyme concentration on reaction rate in which the
effects were tested with three concentrations of both enzyme and substrate (low, medium, and high).After properly setting up the spectrophotometer in
addition to calibration and adding chemicals into the control, enzyme and substrate, one should mix all three concentrations of low, medium, and ...
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Factors include temperature, pH, inhibitors and activators–all of which will be tested and observed for in this lab. The rate of enzyme–catalyzed is
affected by concentrations of both substrate and enzyme. Increasing the temperature on a reaction increases its molecular movement. The rate of an
enzyme–catalyzed reaction increases with temperatures but only up until the point of optimum temperature–the highest point before the eventual
decline. Below the optimum temperature, the hydrogen bonds and hydrophobic interactions that make the enzyme its given shape can no longer be
supported by its flexibility. High temperatures cause enzymes to denature–to lose its three dimensional figure. The denaturation of enzymes plays a
huge role in this lab's absorbance derived from the results. Inhibitors also play a vital role in what affects enzyme functions done in Lab Weeks 4 and
5. When a substrate that binds to an enzyme and the activity decreases, it is called an inhibitor. In our lab, our enzyme inhibitor is hydroxylamine.
Based on the results in a brief statement, the absorbance rate decreases. These results will be delved into deeper analysis further in the

The Type Of Biomolecules Known As Enzymes
Part A: This experiment was based on the type of biomolecules known as enzymes. These molecules found in all living things, and are crucial for the
removal and decomposition of harmful chemicals, the digestion of molecules in metabolism, and the synthesis of proteins, DNA, RNA, and many
other organic molecules. Several key features about enzymes (which are similar to catalysts found in chemistry, only enzymes are organic molecules
that are made of proteins or RNA) is their reusability; an enzyme will never be consumed in a reaction, rather it orients the molecules that would
ordinarily perform the reaction correctly to minimize the energy needed and helps induce the reaction to take place faster. Most enzymes can catalyze
thousands to millions of the same reactions in a second; they are very efficient at the role they perform, Also critical is the substrate, or the molecule
that has to undergo the reaction, which will fit into the active site of the enzyme (a very specific geometric interaction) in order for the reaction to
occur. Each enzyme is only designed to catalyze one type of reaction between very few substrate molecules; this specialization is what makes the
enzymes so efficient. Of course, still being tied to a chemical reaction, the rate of the catalyzed reaction will speed up or slow down depending on
several factors; these include temperature, pH, salinity, solvent, and in the case of this experiment, substrate concentration and enzyme concentration.
The

Enzymes : Proteins That Serve As Biological Catalysts Essay
Brian Bui A3 9/11/16
Enzyme Lab
Introduction
Enzymes are proteins that serve as biological catalysts in a wide variety of life sustaining chemical reactions that take place in cells. A catalyst affects
the rate of chemical reactions, by lowering the activation energy required to make the reaction occur. In an enzyme–catalyzed reaction, a substrate is a
molecule that temporarily binds with the enzyme at an area on the enzyme called the active site. Each enzyme catalyzes only one specific reaction
because there is only one type of substrate molecule that fits perfectly in an enzyme's active site. The substrate temporarily joins with the enzyme to
form an enzyme substrate complex. The substrate is then converted to its products and the enzyme is released. The process is then repeated with
another substrate molecule. Different conditions may change the how the enzyme catalyzes, either making it slower, faster, or not catalyzing at all.
The purpose of the enzyme lab is to measure the enzyme rate in different conditions, the pressure of the enzymes, and how much hydrogen peroxide is
used in a chemical reaction.
Hypothesis
For the floating disk method, if the temperature of the potato enzyme solution is lowered, then the time it takes for the disk to reach the top will be
longer, meaning the enzyme rate will be lower.
Materials
Floating Disk Method:
Raw Potato Pieces
Cold Water
Blender
Test tube
1.5% Hydrogen Peroxide
Forceps
Paper Disks (12)
Timing Device (seconds)
Container

How Substrate Concentration Affects a Catalase Enzyme...
Biology HL
20/9/2013
How Substrate Concentration affects a Catalase Enzyme Reaction
RQ
How does changing the substrate concentration affect the rate of a catalase reaction in an enzyme? Hydrogen peroxide was used as the substrate and
the rate was measured by oxygen production.
Hypothesis
If the substrate concentration is increased then the rate of a catalase reaction will also increase until it reaches the optimal concentration or saturation
point and will remain constant. This is because there will be more substrate molecules in a higher concentration therefore a higher frequency of
collisions. This increases enzyme activity and more product will be formed. However at a certain concentration the enzymes will become saturated (all
... Show more content on Helpwriting.net ...
(0.6 + 0.4 + 0.4)/3 = 0.47
Range of the Rates
Maximum value – minimum value = range eg. Rate of Reaction
Volume ofoxygen produced/time (5 minutes) = R.O.R
e.g.
Standard Deviation – Calculate using Microsoft excel
Percentage Uncertainty
(half the range/rate of reaction value) x 100
e.g.
Data Processing
Conclusion and Evaluation My graph shows there is an almost perfect positive correlation between the hydrogen peroxide concentration and the rate of

the catalase enzyme reaction, with a correlation coefficient of 0.99. The rate of reaction at 1% concentration was 0.46cm3 oxygen produced per
minute and the lowest recorded rate. For 3% was 1.33cm3 per minute, and for 6% was 2.17cm3 per minute and was the highest recorded rate. The

Effect Of Substrate Concentration On Enzyme Activity
The Effect of Environmental Conditions on Enzyme Activity
Ikram Hassan
SBI3UW–02
November 13, 2017.
Research Question: What is the effect of substrate concentration (as measured in % concentration) on the rate of enzyme activity (as calculated by the
dividing the measured distance in cm, +/– 0.1 cm, travelled by a substance in a manometer by the time in seconds, +/– 0.5 seconds)?
Background:
A substrate is a molecule which is acted upon by an enzyme. For a chemical reaction to occur through enzyme, substrate molecules bind to the active
site of an enzyme, which contains residues that catalyse the reaction of the substrate.
Hypothesis: If the concentration of the substrate is increased, then the rate of enzyme activity will decrease. This is because as the concentration of the
substrate increases, there is an increasing amount of occupied active sites at any given moment. This will cause a decrease in the rate of enzyme
activity as substrate–active site collisions are increasingly slowed down thus bringing down the rate of enzyme activity.
Variables:
Independent: Substrate Concentration: Throughout the experiment, the concentration of the substrate used will be increased in order to determine the
effect of an increase of substrate concentration on enzyme activity. The substrate throughout the experiment will be ahydrogen peroxide solution and an
original 30% concentration will be diluted with water into 10% and 5% concentrations in order to observe the effect of

To investigate the effect of surface area on the rate of...
INTRODUCTION
Enzymes are biological catalysts that speed up chemical reactions, without being used up or changed. Catalase is a globular protein molecule that is
found in all living cells. A globular protein is a protein with its molecules curled up into a 'ball' shape. All enzymes have an active site. This is where
another molecule(s) can bind with the enzyme. This molecule is known as the substrate. When the substrate binds with the enzyme, a product is
produced. Enzymes are specific to their substrate, because the shape of their active site will only fit the shape of their substrate. It is said that the
substrate is complimentary to their substrate.
When the substrate binds with the enzyme, it forms an enzyme–substrate complex. The ... Show more content on Helpwriting.net ...
However, temperature difference can affect the experiment. To prevent this, I will conduct the experiment at the same time of day if more than one day
is needed. This is because it is generally colder in the mornings and evening than the afternoon.
Also, I will hold the test tube by the tip. If I were to grab the test tube with my whole hand, my body heat would be passed onto the test tube causing a
temperature increase. Therefore, not creating a reliable set of results.
pH – Enzymes also have an optimum pH level. The pH of a solution affects the enzyme's secondary and tertiary structures. These bonds make the
shape of an enzyme's active site. So, if these bonds are broken, the shape of the active site changes and is distorted. If there is no active site, there is
no reaction resulting in no products. If the enzyme is put in a pH that is very different from the optimum pH, it can cause the enzyme to denature.
Most enzymes have an optimum pH of around 7, which is fairly neutral. To ensure the experiment is a fair test, I will use the same pH of hydrogen
peroxide in every test.
Inhibitors – As mentioned earlier, enzymes have an active site specific to the substrate molecules. However, it is possible for other molecules similar to
enzyme's substrate to bind with the enzyme's active site and therefore, inhibit the enzyme's task.
When the inhibitor binds with the enzyme's active site for a short space of time it is known as competitive inhibition because it is

Lab Report On The Effect Of Substrate Concentration On...
Introduction
The purpose of this lab report is to investigate the effect of substrate concentration on enzyme activity as tested with the enzyme catalase and the
substrate hydrogen peroxide at several concentrations to produce oxygen. It was assumed that an increase in hydrogen peroxide concentration would
decrease the amount of time the paper circle with the enzyme catalase present on it, sowing an increase in enzyme activity. Therefore it can be
hypothesised that there would be an effect on catalase activity from the increase in hydrogen peroxide concentration measured in time for the paper
circle to ride to the top of the solution.
Enzymes are natural catalysts that work from the ability to increase the rate of reaction by decreasing the activation energy of a reaction. (Blanco,
Blanco 2017) An enzyme can do this 10^8– to 10^10 fold, sometimes even 10^15 fold. (Malacinsk, Freifelder 1998) The substrate will momentarily
bind with the enzyme making the enzyme–substrate complex, of which the shape of the substrate is complimentary to the shape of the active site on
the enzyme it is binding with. There are two main theories as to how an enzymes and substrates interact, the lock–and–key model and induced fit
theory. The lock–and–key model suggests that the enzyme has a specific shape that fits the substrate and only that substrate. The induced fit theory
says the active site and substrate are able to change shape or distort for the reaction to take place with (Cooper,

Enzymes And Substrate Concentration
This experiment was conducted to determine the effect of enzymes on its substrate when the quantity of the substrate and the concentration of the
enzyme is altered. More specifically it was looking at how the fat content in the milk is broken down by lipase. At the start of the experiment it was
hypothesised that if 4% lipase solution was added to a mixture of sodium carbonate and bile salts then full cream milk will have a faster rate of
digestion if all variables are kept constant.
Variable 1. Examined how lipase, reacts to different types and amount of fat.
This data refers to the hypothesis as full cream milk had a faster rate of reaction due to the amount of fat present in the milk. This was measured by
using a pH probe as it was ... Show more content on Helpwriting.net ...
As a growing and developing nation scientists have found that lipase can be used in the detergent industry. Microbial lipases are an important group
of biotechnologically valuable enzyme, because of their versatility of their applied properties and ease of mass production (Hasan et al., 2010).
Scientists have discovered that due to lipases microbial origin, and enzymatic properties they are particularly important for industrial use as they can
catalyse a specific reaction. They have been used in the detergent industry as they can reduce the environmental load of detergent products as the
chemical used in conventional detergents and reduced (Hasan et al., 2010). The function of lipases in the detergent industry is to remove fatty residues
and clean clogged drains. This application makes reference to the experiment, as there are many different types detergents on the market, some which
would have a faster rate of reaction. The other real life application which makes reference to the concentration of lipase is, lipase being used in the food
processing, flavor development and improving the quality of food. Through alteration of chemical compounds of vegetable oil with nutritionally
important structured

Substrate And Enzyme
The results of this experiment show me how there must be a balance between the amount of substrate and the amount of enzyme in a reaction. In our
experiment the reaction rate did not increase, it decreased. Because we reduced the amount of substrate in each mixture but kept the amount of enzyme
the same the enzyme cannot react with what is not there. The Yeast (enzyme) was the catalyst in the experiment, and not having the same amount of
substrate did not cause the
5
reaction to take place faster, it caused the enzyme to not be used. This is why the reaction rate of the mixture did not increase it decreased. Therefore
the slope of the reaction declined as we reduced the amount of the substrate in each reaction.
Trial one and two did not produce

The Effect of Substrate Concentration, Enzyme...
Title: "The Effect of Substrate Concentration, Enzyme Concentration, pH and Temperature on Enzyme Activity"
Abstract: In the following experiments we will measure precise amounts of potato extract as well as Phenylthiourea, combined with or without
deionized water and in some instances change the temperature and observe and record the reaction. We will also investigate the different levels of
prepared pH on varying samples of the potato extract and the Phenylthiourea and record the results. We will answer question such as what is the best
temperature for optimum temperature reaction as well as the best pH level for the same reaction.
Introduction: This experiment will entail several areas the first to be investigated will be ... Show more content on Helpwriting.net ...
After measuring equal amounts of distilled water and either adding or subtracting catechol which we referred to as the substrate some reactions was
seen immediately. After which we were able to get data that supported my original hypothesis that in the addition of substrate and anenzyme the
reaction would be present in varying degrees dependent on whether a temperature change was provided or not. In the second part of the experiment
we were testing the inhibition action of Catechol Oxidase at different levels in several tubes of varying samples of potato extract, phenylthiourea
(PTU) and distilled water. The experiment showed that (PTU) bonded with the extract and the water causing a reaction whereas there was no
reaction in tube # 1 where there was an equal amount of everything in the tube. And test tube # 3 was the control tube where the (PTU) was
eliminated as to observe if there was any reaction at all. Of course with the whole experiment we had to be very careful as to add the catechol last to
ensure no premature reaction. It was hypothesized that (PTU) is a non –competitive inhibitor and doubling the substrate will have no reversal effect. In
the exercise # 2 we observed the effect of substrate concentration, enzyme concentration, pH and temperature on enzyme activity. All the data showed
that once potato extract was added to catechol and water the reaction varied dependent on the level of catechol. As in

Enzyme Lab Report
Enzymes are proteins that function as biological catalysts. They can spontaneously metabolize a metabolic reaction without involving itself in the
process. In order for a reaction to start a substrate must be present. As substrate concentration increases so does the initial rate of reaction. However,
as observed in figure 1 , over time all the enzymes will be used up thus saturate and a plateau of a reaction will occur.
Enzymes have sites on their surface which substrates bind to, creating an enzyme–substrate complex. The region into which the substrates bind to are
specific and are referred to as the active site. Suggesting that enzyme–substrate are complementary and should fit together. Theories such as the lock
and key and induced fit depict the substrate–specific nature of enzymes.
Lock and Key Theory
The lock and key theory as seen in Figure 2 states that the substrate molecules will only bind to the enzyme if it passes ... Show more content on
Helpwriting.net ...
The enzyme will continue to change shape until the substrate is binded to it. The theory also states that there are two sites for products to be created
and that is once the substrate is binded to the active site, another site will become active and will then begin the transition of the enzyme–substrate
complex to an enzyme–product.
Thus once a substrate binds to an enzyme, this allows enzymes to catalyse a reaction. This catalysis proceeds in random motions. The products created
by the enzyme–substrate complex are released as another molecule or broken down, thus enabling the enzyme for reuse until it denatures.
Catalase and Hydrogen Peroxide
For this report, catalase in yeast will be used as an enzyme and hydrogen peroxide as a substrate. The expected reaction is that:
2H2O2 в†’ 2H2O +

Rational Engineering Of Dynamic Crystals With A Wide...
Objective 3: Rational engineering of dynamic crystals to fit a wide variety of enzymes and substrates.
The previous objectives dealt with build dynamic crystals and modeling it dynamics. In objective 3, we will customize the dynamic crystals for a wide
range of enzymes and characterize design principles needed to operate multiple modules of crystals, each containing different enzymes, in one pot. This
will be a step towards making scalable multi–modular circuits.
Task 1: The strand interactions for self–assembly of the crystal are shown in Figure 3aa. The double stranded domain to which the green 'spacer strand'
is bound can be increased in length to increase the cavity size of crystals. But one cannot expect to keep extending the ... Show more content on
Helpwriting.net ...
The latter can be characterized by testing if we can successfully conduct a strand displacement reaction (described in Objective 1, task 1). We can
compare the kinetics of strand displacement within the large cavity crystals to the results from the original crystal design used in Objective 1. Larger
cavity sizes should theoretically increase the diffusion rate and hence the rate of strand displacement. These experiments will be repeated for a large
number of crystals for each spacer length and variation in the kinetics of strand displacement between crystals (after normalized for crystal sizes) will
be characterized. The above experiments will establish the upper bound of the cavity size that we can use.
Task 2: Once we arrive at the upper–bound of the crystal cavity size, we will use computational models of these crystals to screen for large number of
candidate enzymes that we can successfully encapsulate within the crystal lattice. (Gaurav) Large–scale screening of enzyme databases. How does their
size and surface charge affect their viability in the crystals?
Once we identify a list of candidate enzymes that are predicted to be compatible with the crystal lattice. The first step would be to check viability of
the crystals in the reaction buffers and temperatures compatible with each of the enzymes. To test this, we will again use the strand displacement

Effect Of Enzyme Lab Report
Enzymes and Factors That Affect Them Rewrite title
Zuryab Rana
October 21, 2017
Abstract:
In the experiment we used Turnip, Hydrogen Peroxide, Distilled Water, and Guaiacol as my substances. On the first activity, Effect of Enzyme
concentration of Reaction Rate for low enzyme concentration, we tested three concentrations of the turnip extract, and hydrogen peroxide. For the
Turnip Extract I used 0.5 ml, 1.0 ml, and 2.0 ml. For hydrogen peroxide we used 0.1 ml, 0.2 ml, and 0.4 ml. We used a control to see the standard, and
used a control for each enzyme concentration used. The control contains turnip extract and the color reagent, Guaiacol. We prepared my substrate tubes
separately from the enzyme tubes. My substrate tube ... Show more content on Helpwriting.net ...
I put one test tube for each control, substrate, and enzyme in the 4В° C (ice bath), 23В° C (room temperature), 37В° C (body temperature), and 60В°
C (water bath). Add the inhibitor that was used and what it was used for.
Introduction:
Enzymes are biological catalysts, which means it decreases activation energy in reactions. The lower activation energy in a reaction, the faster the
reaction rate. Many enzymes alter their shape when they bind to the activation site. This is called induced fit, meaning for the enzyme to work to its
full potential it has to change shape to binding substrate. The location of enzyme's activation site is on the surface of the enzyme, where the binding of
substrates take place. Enzyme activity can be influenced by a variety of environmental factors. If the concentration of enzyme is low, and there is a
great deal of substrate, then increasing enzyme concentration results in more molecules available to convert substrates to products. Thus, increasing
enzyme concentration can increase reaction rate. If substrate concentrations are low, and many of the existing enzymes are idle because of a lack of
substrate, then adding enzyme will have no effect on reaction rate. Enzyme concentration affects the enzyme activity, because the more enzyme
concentration the faster the reaction rate, until it hits it's limiting factor. When substrate concentration is increased, it also increases rate of reaction.
Temperature plays an important

Why Does The Concentration Of An Enzyme Formed Increase...
The concentration of PNP formed increase with time, The reason behind this is because enzymes are powerful catalysts. They can accelerate the
reactions by a factor of as much as a million or more. In this experiment, with the lapse of time, more substrate binds to the enzyme's active site of
which the surface is lined with amino acid residue with substitute groups that bind the substrate and catalyse its chemical transformation. Enzyme
reduced the activation energy of this reaction. This enzyme–catalysed reaction takes a different 'route'. The enzyme and substrate form a reaction
intermediate. Its formation has a lower activation energy than the reaction between reactants without a catalyst. Therefore more PNP formed.
The rate of an enzyme–catalysed

The Effect Of Substrate Concentration Of Hydrogen Peroxide...
The effect of varying the substrate concentration of hydrogen peroxide on the rate of enzyme activity of catalase from potato peel.
Aysha Shahimi, and Jianyi Liang
Department of Biology, Glebe Collegiate Institute. Ottawa, Ontario
Abstract:
The purpose of this lab was to study the effect of varying the substrate concentration of Hydrogen peroxide (H2O2) on the rate of peeled potato catalase
enzyme activity, on the decomposition of H2O2. This experiment was carried out by diluting the 6% H2O2 with distilled water to decrease the
concentration, and then placed in a test tube. A small piece of filler paper disc was coated with the enzyme before it was submerged to the bottom of
the substrate hydrogen peroxide solution. The stop timer was started immediately when the filter paper disc touched the bottom and the timer was
stopped when the filter paper reached the surface. The results of the experiment showed a linear correlation between concentration of the substrate and
the rate of enzyme activity. Overall, as the concentration of H2O2 was decreased, the rate of reaction had decreased.
Introduction:
This experiment was used to determine the effect of varying concentration of hydrogen peroxide on the rate of enzyme activity. This was a
decomposition reaction of hydrogen peroxide into water and oxygen gas. The hypothesis of this reaction is that, the rate of reaction will decrease with
the decrease of hydrogen peroxide concentration.
Enzymes are proteins that act as

Lab Report On Enzyme
Enzyme Lab
Majesty Collins
September 26, 2017
Finding the Greatest Amount of Product with a Spectrophotometer
Introduction For the enzyme experiment, I hypothesized that test tube number one would have the greatest amount of product. My lab partners and I
believed that number one would have the most significant amount of product because it had the highest mL amount of the potato extract. The potato
extract is the enzyme of the investigation being used which is catecholase (Picture 4). The substrate in the investigation is catechol (Picture 6), and the
reddish–brown product is called benzoquinone (Figure 2). Enzymes are proteins that help the speeding up of chemical reactions. Enzymes will never
destroy unless pH, salt, and temperature negatively affect it. When the enzyme is finished with one substrate, it moves on to another one directly after.
According to the lab manual by Pearson (2011), substrates are the reactant molecules that are being changed by the enzyme. It is known that when the
substance is an enzyme, it ends in letters "ase." Substrates and enzymes have a lock and key relationship with one another. The key in the relationship
is the substrate, and the lock in the relationship is the enzyme (Cap, 2016). An example of an enzyme and substrate relationship is sucrase and sucrose.
The enzyme sucrase positions the sucrose, which is table salt, in a way that it can be broken down into the parts of glucose and fructose (Figure 1). The
purpose of this

Structural Similarities Between Enzymes And Substrate
An enzyme is a protein that increases the rate of a chemical reaction by lowering the activation energy of the reaction. This enables the reactant
molecules to intake sufficient amount of energy to reach the transition state. The reactant that an enzyme acts on is referred to as the substrate. After
the substrate molecule binds to an enzyme to form an enzyme–substrate complex, the enzyme converts the substrate to products of the reaction. The
reaction that is catalyzed by an enzyme is very specific meaning that the enzyme will only bind to its specific substrate. For example, sucrase, an
enzyme, will only bind to sucrose molecule. This specificity is due to a molecular recognition mechanism and it operates through conformational as
well as structural similarities between the enzymes and the substrate. ... Show more content on Helpwriting.net ...
Enzyme inhibitors are known for hindering the action of enzymes. Many of the inhibitors simply attach to the enzymes through weak interactions
resulting in reversible inhibitions. In the case of competitive inhibition, inhibitor molecules resemble and mimic the normal substrate molecules and
compete with the the substrate for its attachment to the active site of the enzyme. This simply blocks the substrates from binding to the active site
leading to an impeded enzymatic reaction. In contrast, a noncompetitive inhibitor does not necessarily compete with the substrate to bind to the active
site. It bind to a different site on the enzyme and alters its shape in such manner that the active site becomes less

Essay On Blowfly Temperature
Investigating the Effects of Temperature on the Rate of Respiration of Blowfly Larvae
This experiment was setup to investigate the effects of temperature on the rate of respiration of blowfly larvae.
Background Knowledge
The maggots involved in this investigation were blowflies at the larval stage of development, and they breathe through spiracles in the anterior and
posterior segments. The respiratory tracts are not as developed at this stage, as the organism is not capable of flight, and so it respires less oxygen
than an adult blowfly. They feed on dead organic matter. The respiration of an organism involves an intricate use of enzymes, and so some knowledge
about them is necessary. ... Show more content on Helpwriting.net ...
However, recent studies point towards the induced–fit hypothesis, which means that the substrate and the enzyme are not identical, yet in the presence
of the substrate the active site changes slightly, in order to make it a more "snug" fit. These theories pertain to a further point – the fact that an enzyme
is specific; the majority just have one possible type of substrate molecule. An increase in temperature affects the rate of an enzyme–controlled reaction
in two ways. First of all, the kinetic energy of all of the molecules is increased, thus increasing their speed. If they move faster, they have more
chance of an enzyme colliding with a substrate molecule, and so reacting. This is known as collision theory. The increase of rate can be determined by
the Q10 law. This states that for every 10 degrees in temperature in an enzyme–controlled reaction, the rate of that reaction will double, until 40 degrees
is reached. After this point, the enzyme may start to denature. This is when a certain factor affects the bonds holding the amino acids together, and they
start to break, eventually resulting in the enzyme unravelling. Generally this occurs between 40 and 60 degrees.
Equipment List
* Respirometer (already assembled)
* Blowfly larvae
* Balance

* Soda lime
* cotton wool
* 250ml

Effects of Temperature, Ph, Enzyme Concentration, and...
Effects of Temperature, pH, Enzyme Concentration, and Substrate Concentration on Enzymatic Activity
INTRODUCTION
Enzymes, proteins that act as catalysts, are the most important type of protein[1]. Catalysts speed up chemical reactions and can go without being
used up or changed [3] Without enzymes, the biochemical reactions that take place will react too slowly to keep up with the metabolic needs and the
life functions of organisms. Catecholase is a reaction between oxygen and catechol [2]. In the presence of oxygen, the removal of two hydrogen
atoms oxidizes the compound catechol, as a result of the formation of water [2]. Oxygen is reduced by the addition of two hydrogen atoms, which also
forms water, after catechol is ... Show more content on Helpwriting.net ...
The hypothesis is as the substrate concentration has an increase so will the reaction of velocity if the amount of enzyme is kept constant.
MATERIALS AND METHODS To study the effects of temperature,pH, enzyme concentration, and substrate concentration there were certain steps
that were followed in order to conduct this experiment. Each factor had a separate procedure to follow to find how each had a different effect on the
enzyme.
To find the effect of temperature on the activity of an enzyme, the experiment deals with the steps as follows. First, 3 mL if pH 7 phosphate buffer
was used to fill three different test tubes that were labeled 10, 24, and 50. These three test tubes were set in three different temperature settings. The
first test tube was placed in an ice–water bath for ten minutes until it reached a temperature of 2В° C or less. The second tube's temperature setting
was at room temperature until a temperature of 21В°C was reached. The third tube was placed in a beaker of warm–water until the contents of the
beaker reached a temperature setting of 60В° C. There were four more test tubes that were included in the procedure. Two of the test tubes contained
potato juice were one was put in ice and the other was placed in warm–water. The other two test tubes contained catechol. One test tube was put in ice
and the other in warm water. After

P-Nitrophenol Lab Report
Enzymes
Georgia Canfield
Bio 4811.01
Shazia Ahmed
October 11,2017
ABSTRACT
Our class designed an experiment in order to test the ability of the enzyme cellobiase to break down cellobiose, in order to produce p–nitrophenol
when certain factors were changed including temperature, pH, and inhibitor concentration as well as a change in concentration in the enzyme and
substrate. A baseline experiment was established and absorbances were taken in order to determine the concentration of p–nitrophenol in each scenario.
We then took these calculations in order to then calculate Vo, inhibitor, enzyme and substrate concentration to produce a graph.
Baseline Experiment
TubeTime (min)Absorbance (nm)p–nitrophenol 1100.000 220.0250.210 440.050.413 660.10.745 880.21.471
Following the instructions from the Biofuel Enzyme Kit, we performed a baseline experiment in which all factors remained constant except time in
order to establish a control for absorbance and concentrations of p–nitrophenol. We then used this information to determine the Vo and the other
concentrations in order to form a graph. On a molecular level, since the temperature, pH, inhibitor,

Investigating The Amount Of Enzyme That Would Produce A...
To begin the lab, part A was performed to determine the amount of enzyme that would produce a reaction rate that did not proceed too slow or too
rapidly. As seen on page 13 of the Lab Handout, varying amounts of tyrosinase and phosphate buffer were added to a cuvette while the amount of the
L–DOPA was constant. After all reagents were added to the cuvette, the cuvette was inserted into spectrophotometer and absorbance ofproduct
formation at 475 nm was recorded for two minutes at fifteen seconds interval. After absorbance of product formation was measured and recorded for
each cuvette, as shown on page 14 of the Lab Handout, graphs of rate of production formation versus time, were made with the data of each cuvettes
and the ... Show more content on Helpwriting.net ...
After obtaining all of the absorbance values and unit conversions were calculated, as shown on page 18, a rate of product formation versus time was
graphed as well as a Michaelis–Menten plot. Based upon the Michealis–Menten plot, estimated values of Vmax and Km were recorded. Instead of
generating a Lineweaver–Burke plot to determine the calculated values of Vmax and Km, our lab instructor provided a video for us to watch, which
allowed us to determine the calculated values of Vmax and Km right on the Excel program which were then recorded into our lab notebook. We were
then able to calculate out kcat value and our catalytic efficiency using the equations provided on page 20 of the The same experiment was repeated for
part C of the lab, however, three different data sets were recorded. The first data set contained the addition of DMSO, a second data set had the addition
of the inhibitor quercetin, while the third data set contained fruit extract. The concentration of tyrosinase, quercetin, DMSO, and fruit extract were
constant, while concentration of L–DOPA and phosphate buffer differed from each cuvette as recorded on pages 22 and 23 of the Lab Handout. One
modification to part C compared to part A and B is that the volumes of each reagent was cut down by a third due to supplies running low, however,
this did not affect the experiment in any ways. As seen on pages 22– 25 on the lab manual, after linear plots and Michaelis–Menten graphs

Effect of an Increasing Substrate Concentration on Enzyme...
Hui Tzu(Erin) Wang ID:0720052
Effect of an Increasing Substrate Concentration on Enzyme Activity Rate
Abstract
The reaction rate of an enzyme can be affected by many factors, and the purpose of this experiment was to find out how an increasing substrate
concentration influences the rate of an enzyme activity; we obtained data from recording the absorbance of the samples which contain the same amount
of potato juice (enzyme oxidase) and different amount of catechol (substrate) while holding pH and temperature constant. Our findings illustrate that
the rate of enzyme activity is only influenced by substrate concentration at low level of substrate concentration, and as substrate ... Show more content
on Helpwriting.net ...
Table 2. Effect of substrate concentration on enzyme– catalyzed reactions
Absorbance(420nm)
Tube/Trial0min2min4min6min8min 10min
10.1550.2190.2630.3070.3120.334
20.0770.2500.3500.4220.4570.443
30.1480.4550.5730.6030.5930.563
40.4040.6280.6760.6700.6410.583
By looking at figure 1, we noticed that at higher initial substrate concentration, the absorbance increased at a faster speed (for example, in figure 1,
the slope of test tube 3 is greater than the slopes of test tubes 1 and 2 in the first four minutes); and as time proceeded, the slope of each trial
decreased once passed a certain point and became a constant (slope=0) and eventually moved toward a negative value (except for test tube 1).
Discussion
If we viewed the slopes of the trials from figure 1 as the rates of enzyme activity, our results could be interpreted as the following: when in substrate
concentration increased from a low concentration(for example, from test tube 1 to test tube 2), the rate of the enzyme activity increased with the
increase in substrate concentration; but as the substrate concentration increased, the enzyme activity reached a constant rate where all the enzymes
were saturated(slope=0), and increase in substrate concentration would have no effect on the activity rate. Also, the higher the initial substrate
concentration is, the faster the activity rate reached the constant(for example, test tube 3 reached the constant rate 6

Essay Enzyme Substrate Complex
Meera Patel
Enzyme lab
6/3/2013
Assignment 1 :– Effect of Temperature on Invertase Activity, Determining the Starting Velocity.
Enzyme is the fastest known catalyst. They increase the velocity and rate of reactions in living cells. Diverse range of proteins works as enzyme with
their specific temperature point, pH etc. Enzymes react with the molecules known as substrates. Binding site of an enzyme and a substrate is known as
active site. The amount of enzyme present in a reaction is measured by the activity it catalyzes. The relationship between activity and concentration is
affected by many factors such as temperature, pH, etc. Though enzymes are important for biological reactions, certain factors play an important role in
the ... Show more content on Helpwriting.net ...
Once, the enzymatic reaction attains its maximum point, there would be no increase in the rate of the reaction. The optimum value of the inveratse
remains same under any conditions. Enzymatic reaction will not take place if it cannot reach its specific optimum values whether it is pH, temperature,
substrate concentration or any other factor.
Assignment 2:– pH optimum for Invertase
Hypothesis: Differences in the pH will affect the rate of the velocity of the enzyme activity.
What is the optimal pH for invertase activity? Why and how do pH changes affect invertase activity?
Different enzymes have different pH optimal value that shows at which pH value it can work at its best. The optimum pH of the Invertase is around
4.0, which means that at this pH invertase functions properly and maintains the 3D structure and shape. At lower than 4 and higher 4.0 pH, inveratse
gets denatured and its shape is ruptured resulting in the loss of its ability to function properly. From the graph, we can see that it is not active at the pH
lower than 2.0.
Series| Best pH| 1| 4.0|
If the slope of the line to the left of maximum velocity is different from the slope of the line to the right of maximum velocity, explain why this is.
What is responsible for these differences in enzyme kinetics?
There is an difference between the slope of line on right and left of the optimum

The Effect of Substrate Concentration on the Activity of...
The Effect Of Substrate Concentration On The Activity Of The Enzyme Catalase
A Level Biology Project
Aims
This is an experiment to examine how the concentration of the substrate hydrogen peroxide affects the rate of reaction of the enzyme catalase.
Background Information
Enzymes such as Catalase are protein molecules which are found in living cells. They are used to speed up specific reactions in the cells. They are all
very specific as each enzyme just performs one particular reaction.
Catalase is an enzyme found in food such as potato and liver. It is used for removing Hydrogen Peroxide from the cells. Hydrogen Peroxide is the
poisonous by–product of metabolism. Catalase speeds up the decomposition of Hydrogen Peroxide into water ... Show more content on Helpwriting.net
...
To ensure this is a fair test all the variables except for the concentration of Hydrogen Peroxide must be kept the same for all the experiments. Variables
that must not be altered include:–
Temperature, yeast concentration, type of yeast, batch of yeast, volume of yeast, volume of hydrogen peroxide, air pressure and humidity.
When measuring the volumes of Hydrogen Peroxide, Yeast and Water the measurement should be taken by looking at the scale at an angle of 90
degrees to it to avoid any parallax error.
Predictions
I predict that as the substrate concentration increases, the rate of reaction will go up at a directly proportional rate until the solution becomes saturated
with the substrate hydrogen peroxide. When this saturation point is reached, then adding extra substrate will make no difference.
The rate steadily increases when more substrate is added because more of the active sites of the enzyme are being used which results in more reactions
so the required amount of oxygen is made more quickly. Once the amount of substrate molecules added exceeds the number of active sites available
then the rate of reaction will no longer go up. This is because the maximum number of reactions are being done at once so any extra substrate
molecules have to wait until some of the active sites

Design Experiment

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