Question

Describe the effect that boiling had on pepsin and how you could tell that it had that effect.

Answer 1

Boiling denatures pepsin by disrupting its structure, which can be observed by the lack of protein digestion, as proteins are the substrates for pepsin.

Step-by-step explanation:

Boiling denatures pepsin by disrupting the hydrogen and disulfide bonds that hold its tertiary and quaternary structures in place. This results in the unfolding of the enzyme's structure, rendering it inactive. One can tell that pepsin has been denatured due to boiling by observing a decrease or cessation in its proteolytic activity, meaning it no longer digests protein effectively. To determine this, one could perform a basic experiment involving the enzyme and its substrate, where the substrate for pepsin is protein. Under normal conditions, pepsin would break down the protein into smaller peptides, demonstrating its enzymatic function. However, if pepsin has been boiled, the expected reaction would not occur, or would proceed at a significantly reduced rate. This lack of enzymatic activity indicates that the pepsin has been denatured due to the heat.

Answer 2

Pepsin is denatured by high warmth or high pH. Bubbling can denature most proteins by for all time change their tertiary and quaternary structures. Bubbling denatured pepsin. I can tell since it delivered indistinguishable outcomes from the control. The protein was not processed in test tube 1, there was no shading change, and the optical thickness was 0.