L. Milev, L. Vezenkov, L. Yotova
1994
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Journal
Acta Biotechnologica
Abstract
The ability of the enzyme subtilisin DY for the synthesis of derivatives of DL-aspartic acid which are differently N and C-terminal protected and semiproducts of the peptide synthesis was investigated. The enzyme reaction was characterized by high yields and a comparatively short reaction time. Two of the substrates, Z-D,L-Asp-(OMe)2 and PhAc-D,L-Asp-(OMe)2, were hydrolyzed for about 15 min; the reaction time for Boc-D,L-Asp-(OMe)2 was 2.5 h. The values for the MICHAELIS constants obtained for Z-D,L-Asp-(OMe)2 (Km = 0.576 mM) and PhAc-D,L-Asp-(OMe)2 (Km = 0.300 mM) showed a high affinity of the enzyme to the substrates. For Boc-D,L-Asp-(OMe)2 the affinity of the enzyme is considerable lower (Km = 14.07 mM). The results of these investigations can be effectively used for the separation of N-protected derivatives of D,L-aspartic acid and with a high probability also for other amino and racemic forms.