Effects of Normal and Their Branched Alcohols with Structurally Minimal Variation on Kinetic Parameters in Thermolysin-catalyzed Peptide Hydrolysis and Synthesis of N-(Benzyloxycarbonyl)-L-phenylalanyl-L-phenylalanine and Its Methyl Ester

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When higher alcoholic solvents were added to the reaction medium, and the enhancement of the enzyme activity, followed by its reduction then inactivation, were observed in thermolysin-catalyzed peptide hydrolysis and synthesis. The organic solvent content used was less than the saturating concentration in the buffer (i.e., water-organic one-phase system). The kinetic parameters, K_m and k_cat, at the alcoholic concentration giving maximal enzyme activity in these reactions changed linearly with increasing log P values of the alcohols and consequently k_cat/K_m as well. When the branched isomers of alcohols with structurally minimal variation of which log P was equivalent theoretically, were used as annexments, the kinetic parameters were also changed. The results, especially the changes of K_m for each organic solvent, suggested that each alcohol should act at the active site of the enzyme in its own effective mode.
社団法人日本農芸化学会の論文
1995-03-23