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Study of the experimental conditions for the lipase production by a newly isolated strain of Pseudomonas aeruginosa for the enantioselective hydrolysis of (+/-)-methyl trans-3(4-methoxyphenyl) glycidate.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Study of the experimental conditions for the lipase production by a newly isolated strain of Pseudomonas aeruginosa for the enantioselective hydrolysis of (+/-)-methyl trans-3(4-methoxyphenyl) glycidate.
 
Creator Singh, Sawraj
Kaur, Gurmeet
Chakraborti, Asit K
Jain, R K
Banerjee, U C
 
Subject QR Microbiology
 
Description A lipase producing bacterium has been isolated from the soil to enantiospecifically hydrolyze the (+/-)-methyl trans-3(4-methoxyphenyl) glycidate (MPGM), an intermediate in the synthesis of cardiovascular drug, diltiazem. This hydrolysis provided the desired (-)-MPGM in 44% yield with 99% enantiomeric excess. The organism was identified and confirmed as Pseudomonas aeruginosa by 16S rRNA sequencing. The various physiochemical parameters have been optimized for the maximum production of lipase in shake flask. Beef extract was found to be the best nitrogen source for lipase production. The optimized cultivation conditions were 30 degrees C with an initial medium pH 8 in shake flask. Both inoculum age and inoculum concentration have positive effect on the lipase production and (+/-)-MPGM (3 mM) was found to be the optimal inducer.
 
Publisher Springer Science
 
Date 2006-04
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/1028/1/jain2006.4.pdf
Singh, Sawraj and Kaur, Gurmeet and Chakraborti, Asit K and Jain, R K and Banerjee, U C (2006) Study of the experimental conditions for the lipase production by a newly isolated strain of Pseudomonas aeruginosa for the enantioselective hydrolysis of (+/-)-methyl trans-3(4-methoxyphenyl) glycidate. Bioprocess and biosystems engineering, 28 (5). pp. 341-8. ISSN 1615-7591
 
Relation http://www.springerlink.com/content/75853wt2722x4462/fulltext.pdf
http://crdd.osdd.net/open/1028/