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5 Enzymes

Enzymes are biological catalysts that speed up chemical reactions without being consumed, essential for metabolic processes in living organisms. They exhibit specificity for substrates, forming enzyme-substrate complexes, and their activity is influenced by temperature and pH, with optimal conditions necessary for proper function. Denaturation occurs when enzymes lose their shape due to extreme temperature or pH changes, rendering them inactive.
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0% found this document useful (0 votes)
36 views15 pages

5 Enzymes

Enzymes are biological catalysts that speed up chemical reactions without being consumed, essential for metabolic processes in living organisms. They exhibit specificity for substrates, forming enzyme-substrate complexes, and their activity is influenced by temperature and pH, with optimal conditions necessary for proper function. Denaturation occurs when enzymes lose their shape due to extreme temperature or pH changes, rendering them inactive.
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5.1.

1 Enzymes
What Are Enzymes?
 Enzymes are:
o Catalysts that speed up the rate of a chemical reaction without being changed or
used up in the reaction
 an enzyme is like a lock, the active site is the key hole, the
ubstrate is the key;
o Proteins
o Biological catalysts (biological because they are made in living cells, catalysts
because they speed up the rate of chemical reactions without being changed)
o Necessary to all living organisms as they maintain reaction speeds of all metabolic
reactions (all the reactions that keep an organism alive) at a rate that can sustain life
 For example, if we did not produce digestive enzymes, it would take around 2 - 3
weeks to digest one meal; with enzymes, it takes around 4 hours

Enzyme What It Digests Where It Is Made

Amylase carbohydrates pancreas

Trypsin proteins pancreas

Lipase lipids pancreas, duodenum

Maltase carbohydrates duodenum

Peptidase proteins duodenum

How Do Enzymes Work?


Enzyme substrate specificity

 Enzymes are specific to one particular substrate (molecule/s that get broken down or
joined together in the reaction) as the enzyme is a complementary shape to the
substrate
 The product is made from the substrate(s) and is released
Enzyme specificity: lock and key model of enzyme activity

5.1.2 Enzyme Investigations

Investigating the Effect of Temperature on


Amylase
 Starch solution is heated to a set temperature
 Iodine is added to wells of a spotting tile
 Amylase is added to the starch solution and mixed well
 Every minute, droplets of solution are added to a new well of iodine solution
 This is continued until the iodine stops turning blue-black (this means there is no more starch left
in the solution as the amylase has broken it all down)
 Time taken for the reaction to be completed is recorded
 Experiment is repeated at different temperatures
 The quicker the reaction is completed, the faster the enzyme is working
Investigating the
effect of temperature on enzyme activity

Investigating the Effect of pH on Amylase


 Place single drops of iodine solution in rows on the tile
 Label a test tube with the pH to be tested
 Use the syringe to place 2cm3 of amylase in the test tube
 Add 1cm3 of buffer solution to the test tube using a syringe
 Use another test tube to add 2cm3 of starch solution to the amylase and buffer solution, start the
stopwatch whilst mixing using a pipette
 After 10 seconds, use a pipette to place one drop of mixture on the first drop of iodine, which
should turn blue-black
 Wait another 10 seconds and place another drop of mixture on the second drop of iodine
 Repeat every 10 seconds until iodine solution remains orange-brown
 Repeat experiment at different pH values - the less time the iodine solution takes to remain
orange-brown, the quicker all the starch has been digested and so the better the enzyme works at
that pH
Inve
stigating the effect of pH on enzyme activity

Exam Tip
Describing and explaining experimental results for enzyme experiments is a common
type of exam question so make sure you understand what is happening and, for a 7, 8
or 9, can relate this to changes in the active site of the enzyme when it has denatured,
or if it is a low temperature, relate it to the amount of kinetic energy the molecules
have

5.1.3 Enzyme Action & Specificity:


Enzymes are specific to one particular substrate(s) as the active site of the enzyme,
where the substrate attaches, is a complementary shape to the substrate

 This is because the enzyme is a protein and has a specific 3-D shape
 This is known as the lock and key hypothesis
 When the substrate moves into the enzyme’s active site they become known as
the enzyme-substrate complex
 After the reaction has occurred, the products leave the enzyme’s active site as they
no longer fit it and it is free to take up another substrate
How enzymes work
1. Enzymes and substrates randomly move about in solution

2. When an enzyme and its complementary substrate randomly collide - with the
substrate fitting into the active site of the enzyme - an enzyme-substrate
complex forms, and the reaction occurs.

3. A product (or products) forms from the substrate(s) which are then released from
the active site. The enzyme is unchanged and will go on to catalyse further reactions.

5.1.4 Enzymes & Temperature

 Enzymes are proteins and have a specific shape, held in place by bonds
 This is extremely important around the active site area as the specific shape is what
ensures the substrate will fit into the active site and enable the reaction to proceed
 Enzymes work fastest at their ‘optimum temperature’ – in the human body, the
optimum temperature is 37⁰C
 Heating to high temperatures (beyond the optimum) will break the bonds that hold
the enzyme together and it will lose its shape -this is known as denaturation
 Substrates cannot fit into denatured enzymes as the shape of their active site has been
lost
 Denaturation is irreversible - once enzymes are denatured they cannot regain their
proper shape and activity will stop
Effect of temperature on enzyme activity

 Increasing the temperature from 0⁰C to the optimum increases the activity of
enzymes as the more energy the molecules have the faster they move and the
number of collisions with the substrate molecules increases, leading to a faster
rate of reaction
 This means that low temperatures do not denature enzymes, they just make them
work more slowly
Graph showing the effect of temperature on the rate of enzyme activity

5.1.5 Enzymes & pH


 The optimum pH for most enzymes is 7 but some that are produced in acidic
conditions, such as the stomach, have a lower optimum pH (pH 2) and some that are
produced in alkaline conditions, such as the duodenum, have a higher optimum pH
(pH 8 or 9)
 If the pH is too high or too low, the bonds that hold the amino acid chain together to
make up the protein can be destroyed
 This will change the shape of the active site, so the substrate can no longer fit into it,
reducing the rate of activity
 Moving too far away from the optimum pH will cause the enzyme to denature and
activity will stop
Effect of pH on enzyme activity

Graph showing the effect of pH on rate of activity for an enzyme from the
duodenum
Summary

 Enzymes are biological catalysts. They speed up biochemical


reactions.
 Enzymes are involved in most of the chemical reactions that take
place in organisms.

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