| Autor: |
Qiu J; State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai, 200237, People's Republic of China., Su EZ, Wang HL, Cai WW, Wang W, Wei DZ |
| Jazyk: |
angličtina |
| Zdroj: |
Applied biochemistry and biotechnology [Appl Biochem Biotechnol] 2014 May; Vol. 173 (2), pp. 365-77. Date of Electronic Publication: 2014 Mar 25. |
| DOI: |
10.1007/s12010-014-0845-y |
| Abstrakt: |
In this study, a high (R)-enantioselective nitrilase gene from Sphingomonas wittichii RW1 was cloned and overexpressed in Escherichia coli BL21 (DE3). The recombinant nitrilase was purified to homogeneity with a molecular weight of 40 kDa. The pH and temperature optima were shown to be pH 8.0 and 40 °C, respectively. The purified nitrilase was most active toward succinonitrile, approximately 30-fold higher than that for phenylglycinonitrile. Using the E. coli BL21/ReSWRW1 whole cells as biocatalysts, the kinetic resolution for asymmetric synthesis of (R)-phenylglycine was investigated at pH 6.0. A yield of 46 % was obtained with 95 % enantiomeric excess (ee), which made it a promising biocatalyst for synthesis of (R)-phenylglycine. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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