ENZYMES

PVS THE TUTOR ZAMBIA ONLINE SCHOOL
BIOLOGY 5090
ENZYMES
Enzymes are defined as biological catalysts. A catalyst is any substance that speeds up the rate
of a chemical reaction without itself being changed by the reaction. Enzymes catalyze chemical
reactions in living organisms. Those that work inside of living cells are called intracellular
enzymes while those that work outside living cells are called extracellular enzymes. The
substances on which enzymes act to form products are called substrates. The part of an enzyme
where the substrate fits during an enzyme-catalyzed reaction is called the active site while the
other parts of the enzyme are called allosteric sites. A typical enzyme-catalyzed reaction may be
represented as follows:
Enzyme + substrate enzyme – substate complex enzyme + products
CHARACTERISTICS OF ENZYMES
• Most of them are protein in nature
• They are catalysts
• They catalyze both forward and reverse reactions. That is why the reactants,
intermediates and products in the equation above are linked by half arrows pointing
forwards and backwards.
• They are specific. This means each enzyme acts on only one substrate or a narrow range
of related substrates. Enzyme specificity is discussed latter in this booklet.
• Their activity is affected by temperature, PH, substrate concentration, enzyme
concentration, inhibitors and cofactors (coenzymes and activators).Memory aid: SEPTIC
EXPLANATION OF ENZYME SPECIFICITY

One of the theories used to explain enzyme specificity is called the lock-and-key mechanism.
This theory states that each substrate fits into the active site of a particular enzyme in the same
way a key fits into a specific lock because the two have complementary shapes. The following
diagram illustrates the lock-and-key mechanism.
FACTORS THAT AFFECT ENZYME ACTIVITY
(i) Temperature
Enzyme activity increases with increase in temperature up to the optimum temperature. This
occurs because an increase in temperature results in increase in the kinetic energy of both the
enzyme and the substrate, leading to increased interaction between enzyme and substrate and
formation of enzyme-substrate complex. At temperatures lower than the optimum, the rate of an
enzyme-catalyzed reaction doubles with every increase of 10 o C. The optimum temperature is
the temperature at which an enzyme works best. The activity reduces after the optimum
temperature because the enzyme gets denatured and loses its catalytic function. Enzyme
denaturation is the disturbance of the shape of an enzyme and its active site such that the
substrate no longer fits in the active site. Hence the enzyme can no longer carry out its catalytic
function. The following graph shows how enzyme activity is affected by temperature.
(ii) pH
PH is a measure of how acidic or alkaline a substance is. PH values range from 1 to 14. A PH
value of 7 is said to be neutral. PH values lower than 7 a said to be acidic while values higher
than 7 are said to be alkaline. This means that acidity increases as PH values get lower than 7
and alkalinity increases as PH values get higher than 7. The following diagram illustrates the PH
scale.
The PH value at which a given enzyme works best is called the optimum PH. Values lower or
higher than the optimum PH lower enzyme activity. The optimum PH varies from enzyme to
enzyme, depending on the enzyme’s natural occurrence. For instance, the digestive enzymes of
the stomach work best at acidic PH values while those of the duodenum work best at alkaline PH
values. A graph of enzyme activity against PH is always symmetrical and has its peak at the
optimum PH, as illustrated by the following diagram
(iii) Enzyme Concentration
The rate of an enzyme-catalyzed reaction increases with increase in the concentration of the
enzyme and remains constant when there are no more free substrate molecules for the enzyme to
act on.
(iv) Substrate Concentration
The rate of an enzyme-catalyzed reaction increases with increase in the concentration of the
substrate and levels off (remains constant) when all the enzyme active sites are occupied by the
substrate molecules. Additional substrates have no where to fit on the enzymes.
(v) Inhibitors
An enzyme inhibitor is any substance that slows down or completely stops enzyme activity.
Competitive inhibitors bind to the active site of an enzyme and block the substrate from binding
there. Non-competitive inhibitors bind to allosteric sites of an enzyme and cause the shape of
the active site to change so that the substrate fails to bind. All metabolic poisons are examples of
enzyme inhibitors.
(vi) Cofactors
An enzyme co-factor is any non-protein substance whose presence makes an enzyme active.
Organic cofactors are called co-enzymes e.g. vitamins. Inorganic cofactors are called activators
e.g. mineral salts.
NAMING OF ENZYMES
One way of naming enzymes is using the first part of the substrate name and the suffix –ase,
as illustrated by the following table.
Name of Substrate Name of Enzyme

Carbohydrates Carbohydrase
(i) Starch (amylose and amylopectin) (i) Amylase
( ii ) Maltose ( ii ) Malt ase

( iii ) Sucrose ( iii ) Sucr ase
( iv ) Lactose ( iv ) Lact ase
Proteins Protease
( i) Peptide ( i) Peptid ase
Lipids Lipase
NB: Most protease enzymes have names ending with –in e.g. pepsin, trypsin and rennin.
SOME INDUSTRIAL APPLICATIONS OF ENZYMES
Enzymes have applications in many industries and professions. A few examples are discussed
below.
(i) Making of Biological Detergents

Enzymes are included in biological detergents so that they can hydrolyze stains of biological
origin. The most commonly used enzymes are proteases which breakdown protein stains such as
blood and chlorophyll stains, forming colourless amino acids as products. Lipases and
carbohydrases may be used to get rid of lipid and carbohydrate stains, respectively, but these are
easy to wash even with ordinary detergents.
(ii) Brewing and Baking

Baking and brewing both make use of the enzyme zymase which is found in yeast.
When baking, flour, water, sugar and yeast are mixed to make dough. Yeast secretes zymase
which breaks down sugars to form alcohol and carbon dioxide. The carbon dioxide forms
bubbles which cause the dough to rise.
When brewing cereal seeds are soaked until they start germinating. During the process of
germination, starch is broken down to maltose by the enzyme amylase. Maltose is broken down
to glucose by maltase. The seeds are dried and ground to form a powder. The powder is boiled
in hot water to form a paste. After the past cools, yeast is added. The enzyme zymase from
yeast acts on sugars to form alcohol and carbon dioxide. The alcohol is removed from the
mixture by distillation.
(iii) Making Sweeteners for Food and Drinks

In sweetening of confectioneries, glucose is converted into fructose by the enzyme glucose
isomerase because fructose is sweeter than glucose.
(iv) In the Dairy Industry

In the dairy industry, the enzyme rennin is used to coagulate milk during the making of yoghurt
and cheese.
(v) Tanning of Leather

Tanning is a process by which leather is made soft and pliable. Trypsin is utilized to digest
proteins in the leather during tanning.
(vi) Extraction and Processing of Fruit Juice

When extracting juices from fruits enzymes known as cellulases and pectinases are used to
increase the juice yield and prevent jellying of the juices, respectively.
(vii) Tenderizing of Meat
The meat industry makes use of Trypsin to tenderize meat and predigest baby food.

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PVS THE TUTOR ZAMBIA ONLINE SCHOOL

Enzyme + substrate enzyme – substate complex enzyme + products

EXPLANATION OF ENZYME SPECIFICITY

(iii) Enzyme Concentration

Name of Substrate Name of Enzyme

( ii ) Maltose ( ii ) Malt ase

SOME INDUSTRIAL APPLICATIONS OF ENZYMES

(i) Making of Biological Detergents

(ii) Brewing and Baking

(iii) Making Sweeteners for Food and Drinks

(iv) In the Dairy Industry

(v) Tanning of Leather

(vi) Extraction and Processing of Fruit Juice

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