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Likewise, people ask, what is the pH of pepsin?
Pepsin is most active in acidic environments between 37 °C and 42 °C. Accordingly, its primary site of synthesis and activity is in the stomach (pH 1.5 to 2).
Then, how does pH affect the activity of trypsin?
Between pH 7.0 and 9.5 where the most rapid inactivation takes place, cations soluble at the experimental pH stabilize the enzyme. The affinity of trypsin for cations increases with increasing pH. Complexes of ferric salts with tartrate and pyruvate stabilize the enzyme at pH 8.0.
pH 7 is the optimum pH for amylase. Above pH 7, the activity of amylase rapidly decreases beacuse the concentration of H+ ions (or protons) is too low. This change in [H+] alters the interactions between the variable R-groups of the amino acids in the protein chains that make up the enzyme.