{{asɛmtiNe Ɔkyerɛwfo}} | Nhomakorabea | Nneɛma a ɛma wotumi yɛ ade

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A researcher is studying two enzymes, Amylase and Glycoside Hydrolases, which both catalyze the breakdown of different carbohydrates. Amylase works best on starch, while Glycoside Hydrolases works best on cellulose.
When cellulose is added to a solution containing only Amylase, no reaction occurs. Which of the following best explains this observation?

The activation energy for breaking down cellulose is too high for Amylase.

Cellulose does not fit into the active site of Amylase due to differences in structure.

Amylase becomes denatured when exposed to cellulose.

Amylase lacks the necessary cofactors to break down cellulose.

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The inhibitor changes the enzyme’s shape so the substrate can’t fit at all.

The inhibitor lowers the temperature, which slows down the enzyme’s movement.

The inhibitor adds more substrate, making the reaction slower.

The inhibitor blocks the active site, so the substrate can’t attach to the enzyme.

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The enzyme was used up during the reaction and could not be replaced, because enzymes can only be used once.

The active site moved to a different part of the enzyme to avoid the substrate, causing the enzyme to relocate.

The substrate no longer exists at lower temperatures, causing the substrate to disintegrate.

The enzyme’s shape changed due to changes in the environment, so the substrate no longer fits into the active site.

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The enzyme only works once, but new substrate molecules restore its shape.

The enzyme was replaced by new molecules made during the reaction.

The enzyme was not used up in the reaction and can be reused many times.

The enzyme was permanently changed during the first reaction but still works.