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

Abstract:

: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.

journal_name

Lett Appl Microbiol

authors

Ui S,Takusagawa Y,Ohtsuki T,Mimura A,Ohkuma M,Kudo T

doi

10.1046/j.1472-765x.2001.00869.x

subject

Has Abstract

pub_date

2001-02-01 00:00:00

pages

93-8

issue

2

eissn

0266-8254

issn

1472-765X

pii

lam869

journal_volume

32

pub_type

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