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Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase
Author(s) -
Lee Kong H.,
Lee Pat M.,
Siaw Yew S.,
Morihara Kazuyuki
Publication year - 1993
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280560408
Subject(s) - aspartame , dipeptide , chemistry , elastase , methanol , phenylalanine , enzyme , aspartic acid , kinetics , protease , stereochemistry , biochemistry , amino acid , organic chemistry , physics , quantum mechanics
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.