Step 1: Understanding the Concept:
Enzymatic hydrolysis of proteins often produces hydrophobic peptides that have a bitter taste.
In casein hydrolysate production, a sequential two-stage enzymatic treatment is used to break down these bitter peptides.
Detailed Explanation:
Let us evaluate both statements:
- Assertion (A): During protein hydrolysis, endopeptidases cleave internal peptide bonds, which often exposes hydrophobic amino acids and produces bitter-tasting peptides.
Using a two-stage enzymatic hydrolysis process is the preferred method to break down these bitter compounds and improve the flavor of the final hydrolysate.
Therefore, Assertion (A) is true.
- Reason (R): The reason describes the sequence of the enzymes incorrectly:
1. In the first stage, an endopeptidase is used to break down the intact casein proteins into smaller peptide fragments.
2. In the second stage, an exopeptidase (such as an aminopeptidase or carboxypeptidase) is used. Exopeptidases cleave amino acids from the terminal ends of the peptides, releasing free amino acids and removing the bitter hydrophobic terminal residues.
The Reason statement reverses this sequence, claiming that exopeptidases are used first.
Therefore, Reason (R) is false.
Step 2: Final Answer:
The Assertion (A) is true, but the Reason (R) is false.