Experiment_Effect of pH and Temperature on Enzyme Activity

How do changes in pH and temperature affect the native conformation of an

enzyme?

By changing the ionization states of their amino acid components, pH changes

affect the shape and structure of enzymes. When the ionized states of amino acids
change, the ionic interactions that keep the protein's three-dimensional form are
disrupted, resulting in the enzyme's deactivation. When enzymes are exposed to high
temperatures, however, they become inactive. When the temperature climbs over the
enzyme's ideal operating temperature, the chemical potential energy is strong enough
to break the weak connections that define the proteins' three-dimensional form. As a
result, the protein's function is altered, and the enzyme is rendered inactive.

Define optimum pH and temperature of an enzyme.

The enzyme will operate more slowly if the pH is changed outside of the optimum
range. When enzymes are exposed to excessive pH values, they are denatured.
Temperature impacts enzyme activity in such a way that increasing its temperature
speeds up its activity. This continues until it reaches the optimum temperature for
optimal activity, but when exposed to extremely high temperatures, it loses shape and
stops operating. As a result, the pH and temperature must be below the optimum
ranges for enzymes to reach their maximum activity.

The ideal pH value for an enzyme's maximal activity is defined as its optimal pH.
Enzymes have a variety of ionizable side chains that may be implicated in the active
site, therefore different pH levels impact the structure and activity of the enzyme. The
very top of the graph linking enzyme activity and pH values is the optimal pH. The
optimum temperature, on the other hand, is the temperature range in which the kinetic
energy in enzymes and substrate molecules is optimal for the largest number of
collisions. The temperature is high enough to speed up the reaction while remaining low
enough to avoid denaturing the enzymes at this ideal range.