Catalytic resolution of DL-tryptophan amides using the resting cells of Flavobacterium aquatile ZJB-09211 in a two-phase system

BioChem - DOS

Search

메타 데이터

바이오화학분류

- 바이오플라스틱
  1. 기타
- 바이오정밀화학
  1. 기타
- 화장품용 기능성소재
  1. 기타
- 의료용 화학소재
  1. 식품첨가제

논문

Catalytic resolution of DL-tryptophan amides using the resting cells of Flavobacterium aquatile ZJB-09211 in a two-phase system

학술지

Catalysis communications

저자명

Xu, J.M.; Chen, B.; Zheng, Y.G.

초록

The catalytic activity of Flavobacterium aquatile ZJB-09211 towards the kinetic resolution of DL-tryptophan amides was significantly enhanced by ethyl acetate. A maximum enzyme activity of 5118.62U/g was obtained under the optimized conditions consisting of a mixture of ethyl acetate and Tris-HCl buffer (30:70). In a scale-up reaction, the tryptophan amide concentration was improved to 200mM, with 49.85% (e.e. >99.95%) of the substrate being converted to l-tryptophan. The addition of an organic solvent to the process therefore provided an effective approach for improving the activity of the amidase that could be applied to other amidase-catalyzed bioprocesses.

발행연도

2013

발행기관

Elsevier

ISSN

1566-7367

권

페이지

pp.31-34

DOI

10.1016/j.catcom.2013.04.011

상세정보링크