... splitting of peptide bonds on the carboxyl side of lysine and arginine residues. Therefore the exclusion of trypsin will reduce dramatically the activity of other proteases. It works best at a slightly alkaline pH (pH 7.6-8). This pH is created within the duodenum, by the affects of sodium hydrocarbonate released with the pancreatic juice, in order to neutralize the acidic chyme released from the stomach. The presence of serine amino acid residue in the active site classifies it as part of the serine protease family. Trypsin inhibitors are used as a biological regulatory check upon the activity of trypsin. They are produced by the body in the form of endogenous, and may also be found naturally in seeds, such as beans, and peas. HYPOTHESIS: I believe that as temperature increases so will enzyme activity, until 60°C at which point activity will begin to decrease. This graph demonstrates the predicted stages of ...

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