Stereochemical applications of the expression of the L -2,3-butanediol dehydrogenase gene in Escherichia coli


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Abstract

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.

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