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Activity 1

The document discusses a simulation of enzyme-substrate collisions and how various factors affect reaction rates. It explores how collisions allow reactions between enzymes and substrates and how temperature and pH can impact enzyme activity and denaturation. Key points are made about enzyme specificity, immobilization, optimal conditions, and methods for measuring reaction rates.

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11 views

Activity 1

The document discusses a simulation of enzyme-substrate collisions and how various factors affect reaction rates. It explores how collisions allow reactions between enzymes and substrates and how temperature and pH can impact enzyme activity and denaturation. Key points are made about enzyme specificity, immobilization, optimal conditions, and methods for measuring reaction rates.

Uploaded by

swapnaboddu666
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as DOCX, PDF, TXT or read online on Scribd
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Activity 1 - Simulation of collisions between enzyme and substrate

Experiment with the simulation of collision theory with enzymes


Use this model to investigate the importance of collisions between enzyme and substrate
molecules in enzyme catalysed reactions.
https://www.pedagogie.ac-nice.fr/svt/productions/diastase2/?
maltase=10&maltose=40&ph=7&temp=20&play=1
1. In a first run of the simulation simply observe the way reactions only happen when a substrate
collides with an enzyme
. Enzymes animation Maltase enzymes and maltose sugar
https://www.pedagogie.ac-nice.fr/svt/productions/diastase2/?
maltase=10&maltose=40&ph=7&temp=20&play=1
2. In the second run click on 'Recommencer" which means "Restart", and add some amylose
molecules to the mix.

Enzymes animation Maltase enzymes with maltose sugar and starch (amylose)
Notice that the maltase enzymes have no effect on the amylose - they are substrate specific (they
only hydrolyse maltose)

https://www.pedagogie.ac-nice.fr/svt/productions/diastase2/?
maltase=10&maltose=40&ph=7&temp=20&play=1

3. In a third run click on 'Recommencer" which means "Restart", and this time change the
temperature to 50°C
Enzymes animation Maltase enzymes and maltase sugar at 50°C
Observe the number of denatured enzyme molecules - "Enzymes dénaturée"
https://www.pedagogie.ac-nice.fr/svt/productions/diastase2/?
maltase=10&maltose=40&ph=7&temp=50&play=0

Key points about enzymes


 Enzyme-substrate complex forms through collisions between
substrate molecules and enzyme active sites.
 Sometimes large substrate molecules are immobilized &
sometimes enzymes can be immobilized by being embedded in
membranes. This can reduce the number of collisions.
 The shape of the active site fits only one substrate molecule giving
specificity.
 If the enzyme is denatured the active site changes shape and loses
its ability to catalyse the reaction.
 As the temperature increases, the rate of enzyme substrate
collisions increases, so the reaction rate increases.
 At 50°C the temperature is so high that it breaks some of the bonds
holding the 3D shape of the enzyme - at this point the rate of
reaction falls rapidly because the enzyme molecules become
denatured.
 Optimum pH has the highest rate of reaction.
 As the pH becomes more different from the optimum pH the shape
of the enzyme's active site changes and activity stops when the
enzyme is 'denatured'.

Activity 3 - Simulation of enzyme reactions in different conditions


Biologists often use experiments to study the rate of enzyme catalysed
reactions. One of the easiest methods of estimating the rate of and
enzyme catalysed reaction is to measure the amount of product produced
by the reaction in a given time and then calculate the rate using the
equation,
Rate = products made / time taken.
It is also possible to measure the time taken for the substrate to disappear
and calculate the rate using this formula,
Rate = reactant used / time taken.
In fact the best method of measuring the reaction rate usually depends
on the practical difficulty of measuring a substrate or a product. Gases
are particularly easy to collect because they are liberated from a solution
by the reaction.

The rate of catalase activity is easily measured, without an indicator but


using a measure of the volume of oxygen gas produced.
The rate of amylase is often measured using the disappearance of its
substrate. Iodine solution can be used to measure the presence or
absence of starch, so we can identify the moment when all the starch has
been hydrolysed, because of a colour change in the iodine solution
colour, blue/black becomes yellow/brown.
Trypsin is an enzyme which catalyses the breakdown of protein into
amino acids. Biuret solution can be used to measure the rate of this
reaction.
This Enzyme simulation from Jon Darkow in Ohio provides a great
introduction to factors which affect enzyme reaction rates.
Click the link and follow the steps outlined below.

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