IGCSE Biology

Topic B5: Enzymes

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Useful websites

■ https://igcseaid.com/notes/co-ordinated-scien
ces-0654-2019-21/b4-1-enzymes/

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Syllabus
■ Core
■ Define the term catalyst as a substance that increases
the rate of a chemical reaction and is not changed by the
reaction.
■ Define enzymes as proteins that function as biological
catalysts.
■ Describe why enzymes are important in all living
organisms in terms of reaction speed necessary to
sustain life.

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Catalyst

■ A catalyst is a substance that increases the rate of a

chemical reaction without being consumed (used
up), or changed in the reaction.
■ It is not a reactant.
■ Some metals, (especially transition metals) and their
compounds are good catalysts for particular
chemical reactions in chemistry.

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What are enzymes?
■ Enzymes are biological catalysts - catalysts are
substances that increase the rate of chemical reactions
without being used up.
■ Enzymes are proteins that are folded into complex
shapes that allow smaller molecules called substrates
to fit into them.
■ The place where these substrate molecules fit is called
the active site.

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The speed of enzyme catalyzed reactions

■ An enzyme will speed up the rate of a chemical

reaction many thousands of times.
■ This allows chemical reactions to occur at rates
which would be otherwise be too slow to support life.
■ An increase in temperature of 10◦C approximately
doubles the rate of most enzyme catalysed reactions
(below a certain maximum temperature).

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Reactants and products

■ In a reaction, you generally have two types of chemicals:

the reactants and the products.
■ The reactants react together to form the products.
■ In an enzymatic reaction (a reaction catalysed by an
enzyme), the reactants are known as ‘substrates’.
■ Enzymes work on substrates to form products.

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Syllabus

■ Describe enzyme action with reference to the

complementary shape of an enzyme and its
substrate and the formation of a product (knowledge
of the term active site is not required).

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Enzyme action
■ The place where these substrate molecules fit is
called the active site.
■ However, you only need to state that the shape of a
region of the enzyme is complementary to its
substrate.

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Catalase
■ Catalase is one enzyme present in most organisms
cells.
■ Hydrogen peroxide, which is toxic, may be formed in
cells due to unwanted reactions in respiration.
■ Catalase breaks down (decomposes) hydrogen
peroxide into water and oxygen:

2H2O2(aq) → 2H2O(l) + O2(g)

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Typical enzyme structure (catalase)

■ e

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Syllabus-Supplement

■ Explain enzyme action with reference to the active

site, enzyme-substrate complex, substrate and
product.
■ Explain the specificity of enzymes in terms of the
complementary shape and fit of the active site with
the substrate.

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Mechanism of enzyme action
■ Enzymes have an ‘active site’ – this is the part of the
enzyme that binds to the substrate.
■ Every enzyme’s active site is ‘specific’. This means that
one particular active site can only bind to one type of
substrate.
■ There are several models that explain how enzymes
work - the most important one is the lock and key model.

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The lock and key model
■ Normally, an enzyme will only work on one substrate,
hence the analogy - one lock, one key.
■ The term substrate specificity is used to describe this
specific nature of enzyme action.

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Complementary shape

■ The shape of the active site is ‘complementary’ to its

substrates – this means that the substrate(s) fits into the
enzyme in the same way a key fits into a lock.
■ This complementary nature is what makes the enzyme
specific to a substrate.

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Random collisions
■ In a reaction, the substrate will be randomly moving
around.
■ As a result of this random motion, the substrate will collide
with and bind to an enzyme for which it is specific.
■ This results in the formation of an enzyme-substrate
complex.
■ The enzyme then catalyses the reaction – either breaking
up a substrate (a catabolic reaction) or joining two
substrates together (an anabolic reaction).
■ It then releases the products, to make space for more
substrates, so that the enzyme can catalyse more
reactions.

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Which reaction is anabolic?

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How do enzymes work?
■ After the substrate is bound to the active site, some
bonds within the substrate are weakened (bond strain)
and new bonds may be made, resulting in the formation
of the product(s).
■ The newly formed products are released from the active
site.

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Task

■ Review subtopic 5.1 on pages 46-47 of your

textbook and answer the summary questions.

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Syllabus-Supplement

■ Explain the effect of changes in temperature on

enzyme activity in terms of kinetic energy, shape
and fit, frequency of effective collisions and
denaturation.
■ Explain the effect of changes in pH on enzyme
activity in terms of shape and fit and denaturation.

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 Temperature and enzymes
■ As temperature increases,
so does the rate of reaction.
■ Very high temperatures
denature enzymes.
■ Enzyme activity increases
with temperature until
around 37ºC (body temp.)
■ As the temperature rises
further, the rate of reaction
falls rapidly.

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 pH and enzymes
■ Changes in pH alter an
enzyme’s shape.
■ Different enzymes work
best at different pH values.
■ The optimum pH for an
enzyme depends on where
it works.
■ Intestinal enzymes have an
optimum pH of ~ 7.5
■ Stomach enzymes have an
optimum pH of ~ 2

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Kinetic energy
■ The kinetic energy of an object is that energy that it
possesses due to its motion - the faster it moves, the
higher its kinetic energy.
■ Enzymes bind to their substrates due to the random
motion of the substrates.
■ However, everything in a reaction has kinetic energy –
the enzymes, the substrates, the products i.e. there are a
lot of moving things.
■ Because there are so many things moving around in
random directions, there will be a lot of random
collisions.

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Brownian motion
■ Generally, objects with kinetic energy move in a straight line,
until they collide with something else - then, they either
change direction, speed, or stop moving altogether.
■ This random motion of particles in a fluid resulting from their
collision with other moving particles in the fluid, is called
‘Brownian motion’.

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Brownian motion

■ Due to Brownian motion,

enzymes and substrates will
collide a lot. However, even
when an enzyme and
substrate collide, the
substrate won’t necessarily
bind.
■ A collision that does not
result in the completion of the
reaction is unsuccessful.

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Thermal and kinetic energy
■ As the particles absorb more thermal energy, they move
faster, as thermal energy is converted into kinetic energy.
■ As the particles move faster, there are more collisions in a
given amount of time.
■ As there are more collisions, there are a higher number of
effective collisions in a given amount of time.
■ As there is a higher frequency of effective collisions, the
enzymes catalyse more reactions in a given period of time i.e.
the rate of reaction increases.
■ Once enzymes achieve their maximum activity, they are
working at their optimum temperature.

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Denaturation
■ If you increase the temperature above the optimum,
atoms in the enzymes start to gain too much kinetic
energy to maintain the shape of the enzyme.
■ They vibrate so vigorously that they break the bonds
holding them together, causing the active site of the
enzyme to lose its shape – the enzyme becomes
denatured.
■ As it can no longer bind to its substrate the enzyme can’t
function anymore.

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Changes in enzyme shape - denaturation
■ If the shape of the enzyme changes, its active site may
no longer work - the enzyme has been denatured.
■ Enzymes can be denatured by high temperatures or
extremes of pH.
■ Note that it is wrong to say the enzyme has been ‘killed’ -
although enzymes are made by living things, they are
proteins, and not alive.

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Significance of enzymes

■ Enzymes in cells catalyze:

❑ Photosynthesis

❑ Digestion

❑ Protein synthesis - joining amino acids together

❑ Aerobic respiration

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Task

■ Review subtopic 5.2 on pages 48-49 of your

textbook and answer the summary questions.

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Naming enzymes
■ Can be grouped according to the type of substrate:
❑ Proteases: act on proteins

❑ Carbohydrases act on carbohydrates

❑ Lipases: act on lipids (fats and oils).

■ Others are named by adding the ending ‘ase’ to the

name of the substrate:
❑ Maltase acts on the sugar maltose

❑ Lactase acts on the sugar lactose.

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Classification of enzymes

■ Enzymes can be classified based on the types of

reaction they catalyse.

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Cofactors
■ Cofactors can be divided into two major groups: organic cofactors,
such as flavin or heme; and inorganic cofactors, such as the metal
ions Mg2+, Cu+, Mn2+ .
■ Some enzymes need mineral ions or vitamin cofactors in
order to work properly.

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Syllabus-Core

■ Investigate and describe the effect of changes in

temperature and pH on enzyme activity.

■ Practicals:

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■ FINI

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