Question

why does rennin convert casein into insoluble form?​

Answer 1

Answer:

an enzyme produced in the stomach that coagulates milk. ... Rennin converts caseinogen (milk protein) into insoluble casein in the presence of calcium ions. This ensures that the milk remains in the stomach, exposed to protein-digesting enzymes, for as long as possible.

Rennin, also called chymosin, protein-digesting enzyme that curdles milk by transforming caseinogen into insoluble casein; it is found only in the fourth stomach of cud-chewing animals, such as cows. ... In animals that lack rennin, milk is coagulated by the action of pepsin as is the case in humans.

What effect does rennin have on milk?

Chymosin, known also as rennin, is a proteolytic enzyme related to pepsin that synthesized by chief cells in the stomach of some animals. Its role in digestion is to curdle or coagulate milk in the stomach, a process of considerable importance in the very young animal.

Answer 2

Rennin converts casein into insoluble form.

Explanation:

• Rennin is a proteolytic enzyme related to pepsin that is secreted by chief cells , its main function is to coagulate milk in stomach.
• It is found in infants but absent in adults.
• Coagulation of milk is important in infants because it stops the passage of milk from the stomach.
• It works in presence of calcium.
• It converts casein into paracasein so that it is exposed to protein digesting enzymes , which is later treated by pepsin.