Enzymes are biological catalysts.

There
are optimum temperatures and pH
values at which their activity is greatest.
Enzymes are also proteins, and usually
denatured above about 45C.
Enzymes are important in respiration.
Aerobic respiration releases energy
from glucose.

WHAT ARE
THEY?
As the temperature increases, so does
the rate of reaction. But very high
temperatures denature enzymes.

The graph shows the typical change in
an enzyme's activity with increasing
temperature. The enzyme activity
gradually increases with temperature
until around 37C, or body temperature.
Then, as the temperature continues to
rise, the rate of reaction falls rapidly, as
heat energy denatures the enzyme
TEMPERATURE
AND ENZYMES

A catalyst is a substance that will
change the rate of a reaction.
A catalyst is often used to make a
reaction go faster.
CATALYST
Amylase catalyses the breakdown of starch
into sugars in the mouth and small intestine.

Proteases catalyse the breakdown of
proteins into amino acids in the stomach
and small intestine.

Lipases catalyse the breakdown of fats and
oils into fatty acids and glycerol in the small
intestine.
Amylase, Proteases and Lipases.
-Temperature
-pH
-Allosteric Modulation
-Enzyme Concentration
-Substrate Concentration

*Temperature: As temperature increases past a certain point, the enzymes and proteins (enzymes are a type of
protein) begin to denature due to kinetic disruption of chemical bonds. As temperature decreases, the enzymes are
physically moving around the environment less actively and are taking longer to run into substrates and reactants
(substrates are a type of reactant) and thus take longer to make products.
*pH: As pH number decreases (increase of H+ atoms, or the acidity increases), the H+ atoms attach to the polar
amino acid monomers in the polypeptide making up the enzyme, and disrupt the hydrogen bonds and denature the
enzyme.
*Allosteric Modulation: An allosteric molecule, or an effector (molecule that binds to a protein and effects its
function) can physically change the shape of the enzyme by fitting into an allosteric site and changing the shape of
the active site on the enzyme. "Allosteric interactions can both inhibit and activate enzymes and are a common way
that enzymes are controlled in the body."
There are non-competitive inhibitors, and competitive inhibitors. Non-competitive inhibitors effect the shape of the
active site of the enzyme when settling into the allosteric site. Competitive inhibitors effect the enzyme by settling
into the active site of the enzyme and preventing the intended substrate from fitting in the active site.
*Enzyme concentration: An increase in enzyme concentration will produce an increase in active sites and thus
increase the rate at which the substrate molecules are converted into products.
*Substrate Concentration: If the enzyme concentration is kept constant and the substrate concentration is gradually
increased, the reaction velocity will increase until a maximum rate is obtained.

The factors that affect how well an enzyme works.