CH4: Enzymes

Enzymes and Catalysts

Catalysts: substances that can alter or speed up a chemical reaction, without itself
being chemically changed at the end of the reaction. Inorganic catalysts(ex.
Manganese(IV) Oxide) are not destroyed by boiling/pH changes of the solution.

Enzymes: proteins that function as biological catalysts. They alter or speed up a

chemical reaction, without itself being chemically changed at the end of the
reaction, by lowering the activation energy needed.

Digestion: the process by which large, insoluble food molecules are broken down
into small, soluble and diffusible molecules. Food is digested by digestive
enzymes.

Amylase Digests starch --> maltose

Maltase Digests maltose --> glucose
Protease Digests protein --> amino acids
Lipase Digests fats --> fatty acids + glycerol

How Enzymes Work

Activation energy: The energy needed to start a chemical reaction. Enzymes
lower the activation energy.

Enzymes either:

 build up complex substances(anabolic reactions). Ex: amino acids -->

polypeptides

 break down complex substances(catabolic reactions). Ex: hydrogen

catalase
peroxide --> oxygen + water
Hydrolases: enzymes that catalyse hydrolytic reactions. Digestive enzymes are
hydrolases.

Carbohydrates Digests carbohydrates

Proteases Digests proteins
Lipases Digests lipids(fats)

Enzymes:

 Alter chemical reactions

 Are required in minute amounts: because they remain unchanged in
reactions they catalyse, and so the same enzyme can be reused.
 Are highly specific in action: Ex. amylases only act on starch, not on
proteins or fat, enzyme specificity; each chemical reaction inside a cell is
catalysed by a unique enzyme. The specificity is due to its 3D shape.

'Lock-and-key' hypothesis
Substrate: a substance on which enzymes act. Ex. Protein is the substrate on
which protease acts.

Active sites: depressions on the surface of an enzyme molecule into which the
substrate molecule(s) can fit - like a lock and a key. Reactions converting the
substrate molecule(s) into product molecule(s) take place here.(Enzyme = Lock,
Substrate = Key)

Enzyme-substrate complex: formed when the substrate(s) binds to the enzyme.

Enzymes are affected by temperature
Optimum temperature: temperature at which an enzyme is most active. Usually
about 40-45◦C. Increasing temperature from low to optimum increases enzyme
reaction rate, as kinetic energy is high, chances of the substrate molecule(s) fitting
into the active sites is increased, thereby increasing the rate of the formation of
an enzyme-substrate complex. Increasing the temperature above optimum causes
a decline in reaction rate as the bonds that keep the enzyme protein in shape are
broken.

Enzymes are inactive at low temperature, because at lower temperatures the

kinetic energy is low, and therefore the chances of the substrate molecule(s)
colliding with the enzyme is very low.

Denaturation: the change in the 3D shape of an enzyme/soluble protein, caused

by heat or chemicals(acids/alkalis). The higher the temperature, the faster the
denaturation rate. Denaturation results in the loss/alteration of the enzyme's
active site. The substrate no longer fits into it, so no reaction will occur. The
enzyme can no longer act as a catalyst.

Enzymes are affected by pH

The acidity/alkalinity of the solutions in which enzymes act affect them. Some
work best in acidic solutions(like pepsin in stomach), others work best in alkaline
solutions(intestinal enzymes). Extreme pH changes denatures enzymes.

Enzymes catalyse reversible reactions

Reversible reactions: reactions that can proceed in the forward or backward
direction. Ex. carbonic acid formation from CO2+H2O, catalysed by enzyme
carbonic anhydrase.

CO2 + H2O --> H2CO3

CO2 + H2O <-- H2CO3

(both catalysed by carbonic anhydrase)