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Which consequence results when disulfide bridges are cleaved in pepsin?

A)Enzyme structure becomes globally destabilized
B)Substrate binding affinity increases
C)Catalytic activity instantaneously increases
D)Protein aggregation dramatically is reduced

💡 Explanation

Cleaving disulfide bonds causes widespread destabilization because the covalent cross-linking from disulfide bridges maintains tertiary structure; therefore overall stability reduces rather than catalytic improvement, because the overall structural destabilization hinders specific substrate interactions.

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