Michaelis-Menten Kinetics

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
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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

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

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/Trial 0min 2min 4min 6min 8min 10min
1 0.155 0.219 0.263 0.307 0.312 0.334
2 0.077 0.250 0.350 0.422 0.457 0.443
3 0.148 0.455 0.573 0.603 0.593 0.563
4 0.404 0.628 0.676 0.670 0.641 0.583
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

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; 4°C, 23°C, 37°C, and 60°C. The measurements in this test got higher
as the temperature got higher, but did the measurements under 4°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,

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 2° C
or less. The second tube's temperature setting was at room temperature until a temperature of 21°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 60° 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

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 a hydrogen peroxide solution and
an original 30% concentration will be diluted with water into 10% and 5% concentrations in order to
observe the effect of

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

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 4° C (ice bath), 23° C (room
temperature), 37° C (body temperature), and 60° 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

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

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,

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

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

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

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

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
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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

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
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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 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
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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 an enzyme 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

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

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 of oxygen 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

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

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

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 → 2H2O +

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 ... Show more content on Helpwriting.net ...
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

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 of product 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

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

Enzyme Kinetics of Beta-Galactosidase
Abstract
This experiment is to study and measure the enzyme activity of β–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 β–galactosidase (SIGMA), sodium phosphate buffer pH 7.3
Apparatus: Spectrophotometer (UV–1201), cuvettes, water bath (set at 37°C), 200µl and 1000µl
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
37°C for 5 minutes. 3. The spectrophotometer was set at 420nm. Distilled water was also used as the
'blank'. 4. 200µl of ONPG solutions, which is the

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 ⇄ ES ⇄ EP ⇄ 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 °C, and 60 °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 60°C of warm water. After filling the test tubes with three ml of the

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 a chemical 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

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

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

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
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

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

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

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 ...
Show more content on Helpwriting.net ...
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

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
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

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
Tube Time (min) Absorbance (nm) p–nitrophenol 1 1 0 0.000 2 2 0.025 0.210 4 4 0.05 0.413 6 6 0.1
0.745 8 8 0.2 1.471
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,

Michaelis-Menten Kinetics

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Michaelis-Menten Kinetics