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Proteases as catalysts of enantioselective alpha amino ester hydrolysis 2. pronase catalyzed hydrolysis of tryptophan methyl ester

, : Proteases as catalysts of enantioselective alpha amino ester hydrolysis 2. pronase catalyzed hydrolysis of tryptophan methyl ester. Enzyme and Microbial Technology 3(2): 137-140

The influence of pH, temperature, EDTA and metal ions on the rate of hydrolysis of methyl esters of D- and L-tryptophan by pronase from Streptomyces griseus was studied. pH, Ca2+ and Co2+ have different effects on the hydrolysis of D- and L-substrates, which permits the enantioselectivity of the reaction to be regulated. Maximum enantioselectivity was observed at pH 7 in the presence of 10-3-10-2 M Co2+. The data obtained are compared with the literature data for the hydrolysis of other low MW substrates by pronase. Leucine aminopeptidase may make a considerable contribution to the observed esterase activity of pronase.


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