In the context of enzymes, the difference between the digestion rates observed in Claire's small intestine liquid and her pure protease can be attributed to the concentration and availability of functional enzyme molecules.
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Concentration of Enzymes: Claire's small intestine liquid contains a mixture of various components including enzymes, but the concentration of protease present may be relatively low. Even if proteases are present, there may not be enough enzyme molecules to catalyze the protein digestion effectively, leading to a slower digestion rate.
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Purity and Activity of Protease: The 1 mg of pure protease is concentrated with a much higher population of active enzyme molecules. Since pure protease is likely to be a concentrated source of the specific enzyme responsible for protein digestion, it can easily interact with protein substrates. This leads to efficient and rapid digestion, demonstrating normal enzymatic activity.
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Presence of Inhibitors or Competitive Factors: In the liquid from the small intestine, there may be other factors at play, such as the presence of inhibitors or competitive substrates, that can hinder the protease's action. In contrast, the pure protease has no such complications, allowing it to digest proteins at a normal rate.
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Conditions for Enzymatic Activity: The conditions (such as pH, temperature, and ionic strength) in Claire's small intestine may not be optimal for all the enzymes present, which can further slow digestion. The pure protease, likely tested under ideal conditions, would perform optimally.
In summary, the slower digestion observed in Claire's small intestine compared to the normal rate with pure protease can be explained by factors such as lower concentration of functional enzymes, potential inhibitors, and suboptimal conditions in the intestinal fluid.
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