If pepsin is isolated and placed in a pH 7 solution, it would likely become inactive or exhibit significantly reduced activity. Pepsin is a proteolytic enzyme that is most active in the acidic environment of the stomach, typically around pH 1.5 to 2.5. At a neutral pH of 7, the enzyme's structure may change, leading to a loss of its ability to catalyze the breakdown of proteins efficiently.
the pepsin would become innactive
the pepsin would become innactive
the pepsin would become innactive
Antacids have powerful adsorbent and precipitating effect on pepsin, which can lead to its reduction
Pepsin is an enzyme that primarily breaks down proteins into smaller peptides in the acidic environment of the stomach. If pepsin were mixed with glucose, there would be no significant reaction, as glucose is a simple sugar and not a protein. Pepsin does not act on carbohydrates, so the glucose would remain unchanged in this mixture. Therefore, the interaction between pepsin and glucose would not produce any meaningful biochemical effect.
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Pepsin activity would decrease and at a very low temperature pepsin would be inactive.
Pepsin activity would decrease and at a very low temperature pepsin would be inactive.
When albumin solution, pepsin, and HCl are mixed with biuret reagent, the resulting solution would likely turn purple due to the presence of proteins in the albumin solution. The biuret reagent reacts with peptide bonds in proteins, forming a purple complex. Pepsin is a protease enzyme that can break down proteins, potentially affecting the intensity of the purple color.
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Because Pepsin is the active form of a protein manufactured in the stomach.
Consider the stomach. The inactive form of the digestive enzyme pepsin is called pepsinogin. ( spelling may be wrong ) It takes the release of hydrochloric acid in the stomach to activate this pre-enzyme into pepsin, the active form. You would be digesting your own stomach tissue if pepsin was always active.