Question

In an experiment to study the breakdown of protein, a student uses the enzyme amylase and an indicator. What could be a reason why there is no change in color? A. Protein reacts instantly with amylase and this change cannot be detected by the indicator B. Protein does not react with amylase as it cannot fit into the active sites present in amylase C. The indicator inhibits the reaction between protein and amylase by occupying the active sites of the enzyme D. The indicator becomes inactive upon reacting with protein and cannot indicate the formation of the products

Answer 1

The reason why there is no change in color is that the protein does not react with amylase as it cannot fit into the active sites present in amylase. The correct option among all the options that are given in the question is the second option or option "B". I hope that the answer has come to your help.

Answer 2

Answer:

The correct answer would be B. Protein does not react with amylase as it cannot fit into the active sites present in amylase.

Amylase is an enzyme specifically used in the hydrolysis of glycosidic linkages.

Monosaccharide units are linked with each other with the help of glycosidic bonds in order to form di-, oligo-, and polysaccharides.

There are generally three types of amylase found in nature:

Alpha-amylase (α-amylase): It catalysis the hydrolysis of α-1,4 glycosidic bond. It acts randomly on polysaccharide to yield smaller units such as maltose,  dextrin, and glucose (in case of amylopectin).

Beta-amylase (β-amylase): It also catalysis the hydrolysis α-1,4 glycosidic bond. It cleaves maltose (2 glucose units) from the non-reducing end of the polysaccharide.

Gamma amylase γ-amylase): It catalyses the hydrolysis of α(1–6) glycosidic linkages and last α(1–4)glycosidic linkages at the non-reducing end.

Lastly, breakdown of protein is catalyzes by the enzyme peptidase.