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Stereochemical applications of the expression of the L ‐2,3‐butanediol dehydrogenase gene in Escherichia coli
Author(s) -
Ui S.,
Takusagawa Y.,
Ohtsuki T.,
Mimura A.,
Ohkuma M.,
Kudo T.
Publication year - 2001
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1472-765x.2001.00869.x
Subject(s) - 2,3 butanediol , escherichia coli , stereospecificity , acetoin , gene , biology , gene expression , chemistry , enterobacteriaceae , dehydrogenase , biochemistry , microbiology and biotechnology , enzyme , fermentation , catalysis
S. UI, Y. TAKUSAGAWA, T. OHTSUKI, A. MIMURA, M. OHKUMA AND T. KUDO. 2001 . The L ‐2,3‐butanediol dehydrogenase ( L ‐BDH) gene of Brevibacterium saccharolyticum was strongly expressed in Escherichia coli using the tac promoter. However, the stereospecificity of the resulting L ‐BDH was reduced. The region upstream of the meso ‐BDH gene of Klebsiella pneumoniae was also involved in the expression of the B. saccharolyticum gene. However, in this case, the resulting L ‐BDH exhibited more stable stereospecificity. A stereospecificity recognition region was located within the rear sequence ( Hpa I site, carboxy terminal) of the BDH open reading frame. Using a transformed strain of E. coli , the conversion of L ‐acetoin ( L ‐AC), in the commercially available racemic mixture of AC, to L ‐2,3‐butanediol ( L ‐BD) was attempted. As a result, 0·37% L ‐BD was formed from 1% AC added to the culture.