Document Detail

Improvement of amidase production by a newly isolated Delftia tsuruhatensis ZJB-05174 through optimization of culture medium.
MedLine Citation:
PMID:  19131696     Owner:  NLM     Status:  MEDLINE    
The R-amidase production by a newly isolated strain of Delftia tsuruhatensis ZJB-05174 was optimized in this paper. Effects of factors such as carbon sources, nitrogen sources, and inducers on amidase production were investigated. The medium composition was optimized using central composite designs and response surface analysis. The optimal medium components for enhanced amidase production were found to be as follows: glucose, 8.23 g/l; yeast extract, 11.59 g/l; 2,2-(R,S)-dimethylcyclopropane carboxamide, 1.76 g/l; NaCl, 1 g/l; KH2PO4, 1 g/l; and K2HPO4, 1 g/l. A maximum enzyme production of 528.21 U/l was obtained under the optimized conditions, which was 4.7 times higher than that obtained under initial conditions.
Yuan-Shan Wang; Jian-Miao Xu; Ren-Chao Zheng; Yu-Guo Zheng; Yin-Chu Shen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of microbiology and biotechnology     Volume:  18     ISSN:  1017-7825     ISO Abbreviation:  J. Microbiol. Biotechnol.     Publication Date:  2008 Dec 
Date Detail:
Created Date:  2009-01-09     Completed Date:  2009-07-24     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9431852     Medline TA:  J Microbiol Biotechnol     Country:  Korea (South)    
Other Details:
Languages:  eng     Pagination:  1932-7     Citation Subset:  IM    
Zhejiang University of Technology, 18 Chaowang Road, Hangzhou, Zhejiang 310014, P. R. China.
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MeSH Terms
Amidohydrolases / biosynthesis*
Analysis of Variance
Bacteriological Techniques
Carbon / metabolism
Culture Media / chemistry*
Delftia / enzymology*,  isolation & purification,  metabolism
Glucose / metabolism
Models, Biological
Nitrogen / metabolism
Research Design
Reg. No./Substance:
0/Culture Media; 50-99-7/Glucose; 7440-44-0/Carbon; 7727-37-9/Nitrogen; EC 3.5.-/Amidohydrolases; EC

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