Enzymes

Learning Outcomes:

1. Be able to explain enzyme action in terms of the lock and key hypothesis
o

2. Explain the mode of action of enzymes in terms of:

o Active site
Active site is the region on an enzyme molecule that the substrate binds to.
It is a groove or area on the surface of the enzyme that has a complementary 3-
dimensional structure to the shape of the substrate

o Enzyme-substrate complex
o Lowering of activation energy
o Enzyme specificity

3. Investigate and explain the effects of temperature and pH on the rate of enzyme catalysed
reactions
o Temperature:
At low temperatures, enzymes are inactive and the rate of reaction is very low
Substrate and enzyme molecules have little kinetic energy, hence the frequency of
collision is low
In addition, most substrate molecules do not contain sufficient energy to overcome the
activation energy required to start a reaction

As temperature increases, the rate of enzyme activity increases

This is because the reactants have higher levels of energy, and the substrate molecules
are able to collide with active sites more frequently

At optimum temperature, enzyme activity is the highest

As the temperature increases beyond the optimum temperature, enzyme

activity drops sharply
This is because enzymes are made up of proteins, which are denatured at high
temperatures
The enzyme loses its 3-dimensional structure and active site conformation due to the
breaking of the bonds that hold the structure together

At extremely high temperatures, the enzyme is completely denatured and the rate of
reaction drops to zero

o pH:
Enzyme activity is the highest at the optimum pH of the enzyme
The optimum pH for each enzyme differs E.g.: pepsin (in stomach) works best
under acidic conditions, while intestinal enzymes work best under alkaline
conditions

As the pH increases or decreases from the optimum, enzyme activity sharply

decreases
This is because the hydrogen bonds and ionic bonds that hold the 3-dimensional
structure are disrupted, this the shape of the active site is changed as the enzyme is
denatured

At extreme pH levels, the enzyme is completely denatured and the rate of the
reaction drops to zero
 Enzymes
Enzymes are proteins that function as biological catalysts, and which can alter or speed up the
rate of chemical reactions without themselves being chemically changed at the end of the
reaction

Since enzymes are not consumed by the reaction they catalyse, they can continue to catalyse
more reactions after a reaction is complete
Enzymes work by lowering the activation energy of reactions they catalyse
o Activation energy = Energy needed to start a chemical reaction

Energy

Overall energy change

Time

Contain active sites which are the reactive portions of the enzyme and act on specific
substrates
Digestion is an enzyme-catalysed process Food digested by digestive enzymes (e.g.
Amylase, Maltase, Protease, Lipase)
Enzyme-catalysed reactions can be classified into:
o Anabolic reactions Reactions that build up complex substances
o Catabolic reactions Reactions that break down complex substances
Enzymes can also catalyse reversible reactions (Complex molecules to simpler molecules and
reverse)
Carbonic
anyhydrase
o E.g. CO2 + H2O H2CO3

Enzymes are classified as per the substance on which they act:

o Carbohydrases digest carbohydrates, Proteases that digest proteins, Lipase that digest
lipids (fats)

Characteristics of enzymes
Enzymes speed up chemical reactions
o Enzymes speed up the rate of chemical reactions that occur in the cell by lowering the
activation energy needed to start a reaction

Enzymes are required in minute amounts

 o Because they remain unchanged at the end of the reaction Same enzyme can be used
over and over again to catalyse a large amount of chemical reactions

Enzymes are specific in action (enzyme specificity)

o Highly specific in nature. E.g. amylase on acts on starch, not proteins or fats.
o Specific due to its 3-D shape. Lock and key hypothesis explains how the shape of an
enzyme affects the way it functions

Lock-and-key hypothesis
o Substances which substrates act on are called substrates

o Active sites are depressions on the surface of an enzyme molecule into which the
substrate molecule can fit like a lock-and-key (Enzyme is lock, substrate is key)
o Enzyme has specific 3-D shape, and a specific active site

o Only a specific substrate which is complementary to the active site can fit into the
enzyme.
This results in the formation of an enzyme-substrate complex
o While substrate is attached to the active site, chemical reactions occur. Substrate is
converted into products and later leaves the active site. Enzyme remains unchanged

o General equation is: E + S ES E + P

Where E = enzyme, s = substrate(s), P = product(s)

Factors affecting enzymes

Denaturation is the change of the three-dimensional structure of an enzyme or any other
soluble proteins, caused by heat or chemicals such as acids or alkalis
o Denaturation results in loss or alteration of the enzymes active site. Substrate no longer
fits into enzyme active site and no reaction will occur

Temperature
o Every enzyme has an optimum temperature at which it is most active (Usually 40-45oC)
o Enzymes are inactive at low temperatures
The kinetic energy is low, hence chances of substrate molecule
colliding with enzyme is low
Optimum temperature

o As temperature increases, frequency of collisions

increases as kinetic
energy of molecules increases resulting in
higher rate of reaction
o Enzymes become denatured at very high
temperatures
 Resulting in little or no catalysis, hence rate of reaction decreases
 pH
o Each enzyme can only operate within a narrow range of pH
Acidic or alkaline
E.g. pepsin in stomach acidic environment, intestinal enzymes in alkaline environment

o Beyond the optimum pH range, enzymes become denatured, resulting in little or no

catalysis
o Highest rate of activity of an enzyme is at its optimum pH
Point to note Optimum pH can vary from enzyme to enzyme

Rate of reaction

pH