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The hydrolytic reaction of a protein by trypsin can be demonstrated using the biuret test. In this test, proteins are treated with a solution of copper sulfate and sodium hydroxide, resulting in a violet color if peptide bonds are present. After treatment with trypsin, the breakdown of the protein into smaller peptides or amino acids can be detected as a decrease in the intensity of the violet color, indicating hydrolysis. Additionally, the presence of free amino groups can be confirmed using ninhydrin, which produces a purple color upon reacting with amino acids.

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5d ago

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What might the graph of a pepsin and tryspin indicate about the relative acidity of the stomach of the small intestine?

The graph of pepsin and trypsin activity would likely show that pepsin is more active in acidic conditions, typical of the stomach, while trypsin exhibits optimal activity in a more neutral to slightly alkaline environment, characteristic of the small intestine. This difference indicates that the stomach's acidity facilitates protein digestion by pepsin, whereas trypsin operates effectively when the pH rises after chyme enters the small intestine. Consequently, the graph would highlight the contrasting pH preferences of these digestive enzymes and their respective roles in the digestive process.


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