ISSN:
0138-4988
Keywords:
Life Sciences
;
Life Sciences (general)
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Additional Material:
2 Tab.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/abio.370140314
