A student performs an enzyme experiment at pH 7 and 37°C. She boils the enzyme solution for 10 minutes, cools it back to 37°C, adds fresh substrate, and observes zero activity. When fresh unboiled enzyme is added to the same mixture, full activity is restored immediately. What explains these observations?

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Biology · Enzymology

Verified Solution4 OptionsUpdated: October 2026👁️1 View

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Correct answer

Boiling irreversibly denatured the original enzyme, but left the substrate and cofactors intact for fresh enzyme to act upon.

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Answer 1

Boiling permanently altered the enzyme into a lock-and-key conformation.

Answer 2

Boiling destroyed both enzyme and substrate completely.

Answer 3

Boiling irreversibly denatured the original enzyme, but left the substrate and cofactors intact for fresh enzyme to act upon.

Answer 4

Boiling caused competitive inhibition by denatured fragments occupying active sites.

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