Question

How does pepsinogen change into its active form?

Answer 1

Describe the process of digestion of protein in the stomach. Solution: In thestomach the inactive proenzymepepsinogen when acted upon by hydrochloric acid gets converted into active enzyme pepsin which coverts protein into proteoses and peptides

Answer 2

Answer:

Pepsinogen is converted to active pepsin by Autocatalysis.

Explanation:

Pepsinogen is an inactive enzyme also called Proenzyme or zymogen released from the chief cells of  stomach.

       After being secreted pepsinogen is converted to active pepsin by the removal of 44 amino acids .This process is called autocatalysis.

     The activated pepsin then then act as proteolytic enzyme which helps to cleave the peptide bonds formed by hydrophobic and aromatic amino acids such as tryptophan,tyrosine .