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Enzymes-1

Chapter 5 discusses enzymes as biological catalysts that speed up chemical reactions while remaining unchanged. It covers the mechanisms of enzyme action, factors affecting enzyme activity such as temperature and pH, and differentiates between intracellular and extracellular enzymes. Additionally, it emphasizes the specificity of enzymes and their role in metabolic processes, including anabolism and catabolism.

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0% found this document useful (0 votes)
3 views30 pages

Enzymes-1

Chapter 5 discusses enzymes as biological catalysts that speed up chemical reactions while remaining unchanged. It covers the mechanisms of enzyme action, factors affecting enzyme activity such as temperature and pH, and differentiates between intracellular and extracellular enzymes. Additionally, it emphasizes the specificity of enzymes and their role in metabolic processes, including anabolism and catabolism.

Uploaded by

lim kai wen
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd

Chapter 5

Enzymes
Learning Outcomes
- CORE
- EXTENDED

1. Define enzymes as proteins that function as biological catalysts.


2. Explain enzyme action with reference to the complementary shape of the active site of an enzyme
and its substrate and the formation of a product
3. Investigate and describe the effect of changes in temperature and pH on enzyme activity.
4. Explain the effect of changes in temperature on enzyme activity, in terms of kinetic energy, shape
and fit, frequency of effective collisions and denaturation.
5. Explain the effect of changes in pH on enzyme activity in terms of shape and fit and denaturation.

2018 - 2022 © Tutopiya Pte Ltd


Learning Outcomes
- CORE
- EXTENDED

1. Explain the specificity of enzymes in terms of the complementary shape and fit of the active site
with the substrate
2. Explain the effect of changes in temperature on enzyme activity in terms of kinetic energy, shape
and fit, frequency of effective collisions and denaturation.
3. Explain the effect of changes in pH on enzyme activity in terms of shape and fit and denaturation.

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Types of Reactions in Biological Systems

METABOLISM
Metabolism is the sum of all chemical reactions (anabolism + catabolism) going on within a living organism.

METABOLISM ANABOLISM CATABOLISM

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Types of Reactions in Biological Systems
Anabolic reactions build up large molecules from the smaller ones and usually
ANABOLISM require an input of energy.

Example: Condensation of glucose molecules to form the polysaccharide


glycogen, in the cells of the liver and the skeletal muscles.

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Types of Reactions in Biological Systems
CATABOLISM Catabolic reactions break large molecules into smaller ones and such reactions
are often accompanied with the release of energy.

Example: The breakdown of glucose into carbon dioxide and water by respiration is
an example of catabolism. This takes place in all cells of the body.

All these reactions need biological catalysts called ENZYMES .

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Enzymes
Enzymes are proteinaceous molecules
that function as a biological catalysts.
They speed up chemical reactions
while remaining chemically unchanged
till the end of the reaction.

The molecules that react in the enzyme


catalyzed reaction are called as
SUBSTRATES.

The substances that are produced at


the end of an enzyme catalyzed
reaction is called the PRODUCT.

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INTRACELLULAR VERSUS EXTRACELLULAR ENZYMES

Enzymes are synthesized within living cells.

INTRACELLULAR ENZYMES
Some of them work inside the cells; they are called INTRACELLULAR ENZYMES.

Example: Catalase; it breaks down harmful hydrogen peroxide in liver cells.


Phosphorylase: Builds starch from glucose in plant cells.

EXTRACELLULAR ENZYMES
Some enzymes perform their function outside the cell; they are called EXTRACELLULAR ENZYMES.

Example: Lipase; breaks down fats to fatty acids and glycerol.


Amylase; converts starch to maltose during germination.

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CHARACTERISTICS OF ENZYMES

SUBSTRATE SPECIFIC

Enzymes are specific to their substrate. For example, proteases break down proteins but have no effect
on carbohydrates or lipids, and lipases break down lipids but do not affect proteins or
carbohydrates.

HAS AN OPTIMUM TEMPERATURE

HAS AN OPTIMUM pH

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MECHANISM OF ENZYME ACTION
Lock and Key Hypothesis

• An enzyme is a protein, folded into a complex three-


dimensional shape.

• The active site is the part of the enzyme that allows it to act as
a catalyst.

• Substrate molecules fit exactly into the active site of the enzyme
to form an enzyme-substrate complex, just how a key fits
perfectly into a lock. The active site brings the substrate
molecules closer together.

• The substrates then react to form a molecule of product, which


leaves the active site.

• The enzyme lowers the ACTIVATION ENERGY needed for the


reaction, and the reaction is then much more likely to take
place.

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5. Enzymes
MECHANISM OF ENZYME ACTION

The complementarity in the shape of the


active site of the enzyme and its substrate is
the key to enzyme catalysis.

This indicates that conditions that can


denature enzymes (proteins); such as high
temperatures and pH and alter the structure
of its active site, interferes with the
functionality of the enzyme.

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FACTORS AFFECTING ENZYME ACTIVITY
TEMPERATURE

● An increased temperature means an increased rate of reaction.

● With enzymes, this is true until the optimum temperature of the enzyme is reached.

● The optimum temperature is the enzyme’s ‘favored’ temperature where its work rate is at its maximum.

● Different enzymes have different optimum temperatures.

● An example is human enzymes usually have an optimum temperature of 37°C, which is


the normal body temperature.

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FACTORS AFFECTING ENZYME ACTIVITY
TEMPERATURE

● By exceeding the optimum temperature, the enzyme will be denatured and the rate of enzyme action decreases.

● This is because high temperatures destroy of the bonds that hold the protein structures in the enzyme, thereby
denaturing it.

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FACTORS AFFECTING ENZYME ACTIVITY

pH

● pH affects enzyme function in the same way temperatures does.

● Like optimum temperatures, enzymes also have an optimum pH.

● Optimum pH is the enzyme’s preferred pH to work in, giving its maximum rate of activity.

● Different enzymes have different optimum pHs, depending on their site of action.

○ Pepsin, an enzyme which works in the stomach has a very low optimum pH, because it needs to work in the acidic
stomach environment.
○ Amylase, an enzyme which works in the saliva of the mouth has a fairly neutral optimum pH, as the pH of the mouth is
fairly neutral.

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FACTORS AFFECTING ENZYME ACTIVITY

pH
● Change in pH on either side of the optimum temperature (decrease OR increase) will denature the enzyme.

● This is because extreme pHs destroy the bonds that hold the protein structure, just how extreme temperatures does.

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FACTORS AFFECTING ENZYME ACTIVITY

Activators and Inhibitors


Some molecules change the likelihood of an enzyme being able to bind to its substrate.

● Activators make this binding more likely – for example, chloride ions are essential for the activity of salivary amylase.

● Inhibitors make it more difficult for the enzyme to bind to the substrate - for example, cyanide ions block the active sites of
enzymes involved in respiration.

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INVESTIGATING THE EFFECT OF pH ON ENZYMES
5. Enzymes
EXAMPLE AMYLASE

Amylase breaks down starch to glucose.

Salivary amylase breaks down small amounts of starch to maltose in the mouth.

Pancreatic amylase breaks down the leftover starch to maltose in the intestines.

The difference between the two enzymes lies in their OPTIMUM pH.

Salivary amylase functions in the mouth its optimum pH is 6.8 (The pH of the mouth is slightly acidic; somewhere
between 6-7).

Pancreatic amylase functions in the intestines and its optimum pH is (The pH of the intestines is slightly alkaline;
somewhere between 7-8).

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EXPERIMENT TO DETERMINE THE EFFECT OF pH on AMYLASE

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DIFFERENT ENZYMES AND THEIR FUNCTIONS
Enzymes control a lot of vital processes in an organism, such as respiration, photosynthesis,
digestion, protein synthesis, etc.

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Contents Practice Questions

Q1 Some medicines are made into tablets which are coated in a


starch-like substance. The coating protects the medicine from
the effects of gastric juice. Which enzyme digests the coating
and what is produced by this action?

Enzymes Products
A amylase Fatty acids and glycerol
B amylase Simple reducing sugars
C lipase Fatty acids and glycerol
D lipase Simple reducing sugars

Ans. B
Contents Practice Questions

Q2 Which statement describes the effect of temperature on


enzymes?

A High temperatures denature enzymes making it difficult for substrate


molecules to fit into the active site.

B High temperatures denature enzymes making it easy for substrate


molecules to fit into the active site.

C Low temperatures denature enzymes making it difficult for substrate


molecules to fit into the active site.

D Low temperatures denature enzymes making it easy for substrate


molecules to fit into the active site.
Ans. A
Contents Practice Questions

Q3 Which statement about an enzyme-controlled reaction is


correct?

A During the reaction, the substrate changes into products.

B The enzyme is gradually used up during the reaction.

C The enzyme is slowly broken down during the reaction.

D The higher the temperature, the slower the reaction.


Ans. A
Contents Practice Questions

Q4 Starch is digested by amylase in the mouth, but it is not digested


in the stomach. What is the reason for this?

A All starch digestion is completed in the mouth.

B The pH in the stomach is not suitable for the amylase to work.

C The starch does not stay in the stomach long enough to be digested.

D The temperature in the stomach is not suitable for the amylase to work.

Ans. B
Contents Practice Questions

Q5 The graph shows the concentration of a substance during the


course of an enzyme-controlled reaction.
Which substance is this?

A Enzyme
Concentration
B Enzyme - substrate
complex

C Product Time

D Substrate
Ans. A
Contents Practice Questions

Q6 Enzymes function best at their optimum temperature. Which


statement describes the effect on an enzyme of increasing the
temperature to the enzyme's optimum temperature?

A There are more frequent successful collisions.

B The kinetic energy of the enzymes decreases.

C The enzymes begin to lose their complementary shape.

D The rate at which enzyme-substrate complexes form is reduced.


Ans. A
Contents Practice Questions

Q7 Where in the alimentary canal is the enzyme trypsin found and


what are the products of the reaction it catalyses?

Where Trypsin is found Products


A Duodenum Amino acids
B Duodenum Fatty acids
C Ileum Proteins
D Stomach Amino acids

Ans. A
Contents Practice Questions

Q8 An experiment was carried out to study the effect of


temperature on the time taken for protein to be digested by
an enzyme.
The table shows the results.

Temperature / oC Observation
25 4 hours for complete digestion
35 2 hours for complete digestion
45 3 hours for complete digestion
55 No digestion takes place

For these results, at which temperature does the enzyme denature?

A 20 oC B 30 oC C 40 oC D 50 oC
Ans. D
Contents Practice Questions

Q9 The graph shows the effect of pH on the rate of an enzyme-


catalysed reaction.

ph
Contents Practice Questions

Q9 What explains the effect of pH on the reaction rate?

A As the pH increases from 5 to 7, the kinetic energy increases.

B As the pH increases from 7 to 9, the frequency of enzyme and substrate


collisions increases.

C The shape of the enzyme's active site changes as the pH increases from 7 to 9.

D The substrate denatures at pH 7.

Ans. C
Contents Practice Questions

Q10 Four test-tubes were set up as shown in the diagram.


In which test-tube is the starch digested most quickly?

Ans. C

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