Kinetics of aspartame precursor synthesis catalysed by <i>Pseudomonas aeruginosa</i> elastase

Abstract

Abstract Elastase isolated from Pseudomonas aeruginosa IFO 3455 was found to be an efficient protease to catalyse the synthesis of N ‐benzyloxycarbonyl‐aspartyl‐phenylalanine methyl ester, the precursor of the dipeptide sweetener, aspartame. The influence of methanol as a cosolvent in this synthetic reaction was investigated. It was found that the synthesis of the dipeptide precursor was most efficient in 25% (v/v) methanol, pH 7·0 at about 25°C for a reaction time of about 3 h. However, the activity of the enzyme was greatly reduced in 90% methanol. The values of K and k 2 for N ‐benzyloxycarbonyl‐aspartic acid were 0·17 mol dm −3 and 11·9 mol dm −3 s −1 respectively.