A novel whole-cell biocatalyst with NAD+ regeneration for production of chiral chemicals

The high costs of pyridine nucleotide cofactors have limited the applications of NAD(P)-dependent oxidoreductases on an industrial scale. Although NAD(P)H regeneration systems have been widely studied, NAD(P)(+) regeneration, which is required in reactions where the oxidized form of the cofactor is...

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Bibliographic Details
Published in:PloS one 2010-01, Vol.5 (1), p.e8860-e8860
Main Authors: Xiao, Zijun, Lv, Chuanjuan, Gao, Chao, Qin, Jiayang, Ma, Cuiqing, Liu, Zhen, Liu, Peihai, Li, Lixiang, Xu, Ping
Format: Article
Language:English
Subjects:
Acetoin
Bacillus cereus
Bacillus subtilis
Biocatalysis
Biocatalysts
Biotechnology/Applied Microbiology
Biotechnology/Biocatalysis
Biotechnology/Bioengineering
Butanediol
Catalysis
Chemicals
Cofactors
Dehydrogenases
E coli
Electrophoresis, Polyacrylamide Gel
Enzymes
Escherichia coli
Escherichia coli - metabolism
Glycerol
Hydrogen-Ion Concentration
Kinetics
Laboratories
Lactobacillus
Lactobacillus brevis
Membrane reactors
Multienzyme Complexes - metabolism
NAD - metabolism
NADH oxidase
NADH, NADPH Oxidoreductases - metabolism
Nicotinamide adenine dinucleotide
Oxidation
Proteins
Pyridines
Recombination, Genetic
Regeneration
Stereoisomerism
Substrate Specificity
Trends
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Summary:The high costs of pyridine nucleotide cofactors have limited the applications of NAD(P)-dependent oxidoreductases on an industrial scale. Although NAD(P)H regeneration systems have been widely studied, NAD(P)(+) regeneration, which is required in reactions where the oxidized form of the cofactor is used, has been less well explored, particularly in whole-cell biocatalytic processes. Simultaneous overexpression of an NAD(+) dependent enzyme and an NAD(+) regenerating enzyme (H(2)O producing NADH oxidase from Lactobacillus brevis) in a whole-cell biocatalyst was studied for application in the NAD(+)-dependent oxidation system. The whole-cell biocatalyst with (2R,3R)-2,3-butanediol dehydrogenase as the catalyzing enzyme was used to produce (3R)-acetoin, (3S)-acetoin and (2S,3S)-2,3-butanediol. A recombinant strain, in which an NAD(+) regeneration enzyme was coexpressed, displayed significantly higher biocatalytic efficiency in terms of the production of chiral acetoin and (2S,3S)-2,3-butanediol. The application of this coexpression system to the production of other chiral chemicals could be extended by using different NAD(P)-dependent dehydrogenases that require NAD(P)(+) for catalysis.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0008860