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3: Enzymes
2.3.1 Enzymes are:
globular proteins
The active site is often composed of open loops of polar amino acids on the exterior of the
enzyme molecule.
Enzyme specificity is due to the complementary shape of the active site and the substrate.
Enzymes work at low concentrations because they are unaffected by the reaction and can
return for more substrate.
2.2.3 The effects of temperature, pH and substrate concentration on enzyme
activity( rate of reaction).
(a)
(b)
(c)
enzyme is denatured
The effect of pH
(a)
Specificity reduced
Active site structure and structure specific to the complementary shape of the substrate.
(c)
Increase in pH
Specificity reduced
(a)
(b)
New substrate must wait for previous reaction to complete and the product to exit the
active site
(c)
' a structural change in a protein that results in a loss (usually permanent) of its biological
properties. '
Shape of the active site is maintained by hydrogen, ionic and covalent bonds
The bonds within enzymes (and proteins) has an increasing strength of:
Hydrogen
Ionic
Covalent
• As the temperature increases the stability of the enzyme remains constant. The weakest
• The kinetic energy of both the enzyme and substrate increase. Therefore more activated
BUT
• (The KE of the enzymes constituent atoms has increased and the weakest bonds
(hydrogen bonds)break. The shape of the active site is lost. There is a rapid loss of activity
Enzymes have an optimum pH at which they achieve their maximum rate of reaction or
Vmax
e.g. carboxyl R group will be uncharged COOH at low pH but COO- at high pH.
2.3.5 Commercial applications of enzymes in biotechnology
Biotechnology is the use of micro-organisms or parts of organism to produce a commercial
product. In particular the use of enzymes can reduce production costs to a commercially
viable level. Biotechnology has ancient origins in the production of fermentation products.
There are however an increasing number of modern applications in industry. The follow is an
outline of two such applications.