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Factors Affecting Enzyme Activity
Research · December 2020
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Factors Affecting Enzyme Activity
Research · December 2020
DOI: 10.13140/RG.2.2.27359.48800
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Eman Shrief
Ain Shams University,Women Faculty for Arts, Science and Education
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Factors Affecting Enzyme Activity
Eman Farghly Hassan Shrief
Department of Biochemistry and Nutrition, Ain Shams University, Women Faculty for
Arts, Science and Education.
Received on December 12, 2020.
Abstract
Enzyme activity affected by a variety of factors, such as temperature, pH, and
concentration. Substrate concentration: Increasing substrate concentration also
increases the rate of reaction to a certain point, Effect of Water and effect of
Inhibitors and activator.
Introduction
Enzymes are catalysts or chemical agents that speed up chemical reactions without
being consumed. Most enzymes are proteins that function to reduce energy of
activation in chemical reactions. They work on reactants called substrate; the
enzyme attaches to the substrate and then the enzyme converts the substrate into a
product, while the enzyme remains unaffected. Enzyme activity affected by several
factors that will be discussed below.
2
1. Temperature Effect
As the temperature increases the rate of chemical reaction will increase, but just up
to a certain point, then it will sharply drop.
The optimal temperature it occurs when the rate of the reaction is at its highest,
each enzyme has a certain temperature at which it is more active, ranges between
37 to 40C°.
The protein nature of
the enzymes makes
them extremely
sensitive; so after the
optimal temperature the
rate starts to drop that is
because the protein starts to denature Figure 1.1 Temperature influence on rate of
reaction.
so it loses its shape and don’t function
well.
The enzyme activity gradually lowers as the temperature rises more than the
optimal temperature until it reaches a certain temperature at which the enzyme
activity stops completely due to the change of its natural composition.
On the other hand, if the temperature lowers below the optimal temperature, the
enzyme activity lowers until the enzyme reaches a minimum temperature at which
the enzyme activity is the least. The enzyme activity stops completely at 0C°, but if
the temperature rises again, and then the enzyme reactivate once more. [1, 2]
3
2. PH Effect
Enzymes are protein substances that contain acidic carboxylic groups (COOH–)
and basic amino groups (NH2). So, the enzymes are affected by changing the pH
value.
Each enzyme has a pH value that it works at with maximum efficiency called the
optimal pH. If the pH is lower or higher than the optimal pH, the enzyme activity
decreases until it stops working. For example, pepsin works at a low pH, i.e., it is
highly acidic, while amylase works at a
high pH, i.e., it is basic. Most enzymes
work at neutral pH 7.4. [2]
Figure 2.1. pH influence on rate of reaction.
Figure 2.2. Low pH is commonly found in
stomach enzymes e.g. Pepsin
High pH e.g. amylase
4
3. Concentration Effect
a. Substrate concentration
Increasing substrate concentration also increases the rate of reaction to a certain
point. Once all of the enzymes have bound, any substrate increase will have no
effect on the rate of reaction, as the available enzymes will be saturated and
working at their maximum rate.
b. Enzyme concentration
Increasing enzyme concentration will elevate the
chemical reaction rate, as long as there is substrate
available for binding. Once all of the substrate is
bound, the reaction will no longer speed up,
because there will be nothing for additional
enzymes to bind to.[ 3] Figure 1.3. there is no use of excess
substrate once it all bind with the
enzyme
Figure 3.2 the difference between the enzyme and substrate
concentration upon the chemical reaction rate
5
4. Water effect
To some extent, enzymes need to b hydrated in order to develop activity e.g.
Hydration of Lysozyme was determined by IR and NMR spectroscopy. first the
charged polar groups of the side chains hydrate, followed by the uncharged
ones.
In preservation of food, it is mandatory to inhibit enzymatic activity completely if
the storage temperature is below the phase transition temperature. [4]
5. Activators Effect
Activators they enhance the activity of an enzyme.
Some of the enzymes require certain inorganic metallic cations, like Mg2+,
Mn2+, Zn2+, Ca2+, Co2+, Cu2+, Na+, K+ etc., for their optimum activity.
Compounds which are active as prosthetic groups or which provide
stabilization of the enzyme’s conformation or of the enzyme-substrate complex
Rarely, anions are also needed for enzyme activity, e.g. a chloride ion (CI–) for
amylase. [1, 3, 4]
6. Inhibitors effect
Enzyme activity is inhibited in various ways. Two of them are:
a. Competitive inhibition
Occurs when molecules very similar to the substrate molecules bind to the active
site and prevent binding of the actual substrate.
Penicillin, for example, is a competitive inhibitor that blocks the active site of an
enzyme that many bacteria use to construct their cell walls.
6
b. Noncompetitive inhibition
1. Occurs when an inhibitor binds to the enzyme at a location other than the active
site.
2. In some cases of noncompetitive inhibition, the inhibitor
is thought to bind to the enzyme in a way to block the Allosteric (control)
normal active site.
In enzymology,
3. In other instances, the binding of the inhibitor is believed
inhibition or activation
to change the shape of the enzyme molecule, thereby of an enzyme by a small
deforming its active site and preventing it from reacting regulatory molecule that
with its substrate. This type of noncompetitive inhibition interacts at a site
called allosteric inhibition; the place where the inhibitor (allosteric site) other
than the active site (at
binds to the enzyme is called the allosteric site. Frequently,
which catalytic activity
an end product of a metabolic pathway serves as an
occurs)
allosteric inhibitor on an earlier enzyme of the pathway.
This inhibition of an enzyme by a
product of its pathway is a form of
negative feedback.
Allosteric control can involve
stimulation of enzyme action i.e. ;(
activators) as well as inhibition. An
activator molecule can be bound to an
allosteric site and induce a reaction at the
active site by changing its shape to fit a
substrate that could not induce the Figure 6.1. The competitive and non-
change by itself. Common activators include competitive inhibitors effect on reaction rate.
hormones and the products of earlier enzymatic
reactions. [5]
7
Figure 6.2. Allosteric control can involve stimulation of enzyme
action i.e. ;( activators) as well as inhibition ,as illustated.
A comparison between Enzyme activators and inhibitors
Enzyme activator Enzyme inhibitor
Definition Chemical species can Chemical species can
bind with an enzyme to bind with an enzyme to
increase its activity. decrease its activity.
Effect on enzyme Can increase enzyme Can decrease enzyme
activity. activity.
Examples Include hexokinase-1 and Include drugs,
glucokinase. ribonuclease inhibitor.
8
References
1. https://youtu.be/no36EgNHg6s
2. https://alevelbiology.co.uk/notes/factors-affecting-enzyme-activity
3. https://www.khanacademy.org/science/high-school-biology/hs-energy-and-
transport/hs-enzymes/a/hs-enzymes-review
4. Hassanien, Mohamed. (2012). Factors affecting Enzyme- Catalyzed Reactions.
10.13140/RG.2.2.36798.64328.
5. Contributor: The Editors of Encyclopedia Britannica, Title: Enzymes,
Publisher: encyclopedia Britannica, date Published: December 05, 2019
URL:
https://www.britannica.com/science/enzyme
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