The protease-catalyzed transesterifications between Ntrifluoroacetyl-DL-phenylalanine 2,2,2-trifluoroethyl ester and 1-propanol were studied in a variety of anhydrous organic solvents at 30Β°C. The protease preparations lyophilized from phosphate buffer solutions (pH 8.0) were used as catalysts. The
Effect of ester moiety of substrates on enantioselectivity of protease catalysis in organic media
β Scribed by Katsuhiro Kawashiro; Hideki Sugahara; Tomoya Tsukioka; Shigeru Sugiyama; Hiromu Hayashi
- Publisher
- Springer Netherlands
- Year
- 1996
- Tongue
- English
- Weight
- 417 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0141-5492
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β¦ Synopsis
The a-chymotrypsin-catalyzed transesterification between a racemic N-trifluoroacetylphenylalanine ester and 1-propanol, was carried out in organic media. Although activation of the substrate by introducing electron-withdrawing group to the ester moiety enhanced the rate of reaction, it decreased enantioselectivity at the same time. In the instance of subtilisin Carlsberg, inversion of the L-specificity was observed.
π SIMILAR VOLUMES
A simple methodology has been successfully employed to explain the solvent dependence of the substrate specificity of enzymes in organic media. This methodology, which does not require the knowledge of the enzyme structure and is thus applicable to lyophilized and other noncrystalline enzyme prepara