Question

Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum $pHof7.7to8.0$. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?

a. changing the$pHto3.0$

b. running the reaction at$75°C$

Short answer

Part a) Raising the $pHto3.0$,slows down the reaction.

Part b) The hydrogen atoms and dispersion forces of organic molecules are destroyed so when temperature rises to $75°C$, causing in enzymatic activity.

Step-by-step solution

Introduction (Part a).

Phenyl compounds are linked with benzene and can be regarded of as an aromatic ring with just a hydrogen deleted, that can be supplied by yet another atom or chemical to act as a substituents.

Given Information (Part a).

Enzyme requires accurate circumstances to function in the society, including a particular pH, heat, and so forth. Since the energy of the molecules rises as the temperature goes up, the lipase rises. As both an outcome, the reagents collide greater regularly in order the surpass the energy gap through energy gap. The chemicals demand activation energy to react.

Explanation(Part a).

Alteration of the enzymes arises when the temperature rose too great. Distance from ideal pH also will slow reaction.

(a). The proper pH for trypsin seems to be between $pHof7.7to8.0$. Lowering the acidity to localid="1654235878444" $3.0$causes bogs down the action.

Given data (Part b).

For the systems engineering of aromatase driven processes, a micro-scale technology has now been created.

Explanation (Part b).

(b). The appropriate body temp is around $36°Cand36.5°C$. The hydrogen atoms and electrostatic forces of amino acids were broken so when temperature rose to $75°C$, culminating in nitrification.