Step 1: Understanding the Concept:
Rennet coagulation of milk involves two main stages: an enzymatic stage (cleavage of \(\kappa\)-casein by chymosin) and a non-enzymatic aggregation stage (coagulation of destabilized micelles in the presence of calcium ions).
Step 2: Detailed Explanation:
Let us analyze both statements:
• Assertion (A): When milk is heated to high temperatures, the major whey protein \(\beta\)-lactoglobulin denatures and exposes its free sulfhydryl group. It then interacts with the sulfhydryl groups of \(\kappa\)-casein via disulfide exchange, forming a \(\beta\)-lactoglobulin–\(\kappa\)-casein complex. This complex sterically hinders the access of chymosin to its target cleavage site (Phe105–Met106) on \(\kappa\)-casein, thereby prolonging the rennet coagulation time. This statement is True.
• Reason (R): The enzyme chymosin has a highly acidic pH optimum (around 5.5). As the pH of milk decreases from its normal value (6.7) toward this optimum, the enzymatic cleavage of \(\kappa\)-casein proceeds much faster. This statement is True.
While both statements are scientifically true, the effect of pH described in (R) does not explain the thermal interaction of \(\beta\)-lactoglobulin with \(\kappa\)-casein described in (A).
Thus, (R) is not the correct explanation of (A).
Step 3: Final Answer
Both (A) and (R) are true, but (R) is not the correct explanation of (A).