Expression of the Gene of Glycerol Dehydrogenase from Hansenula polymorpha Dl-1 in Escherichia coli for the Production of Chiral Compounds

Yamada‐Onodera, Keiko; Yamamoto, Hiroaki; Kawahara, Nobuhiro; Tani, Yoshiki

doi:10.1002/1521-3846(200207)22:3/4<355::aid-abio355>3.0.co;2-6

Cited by 25 publications

(20 citation statements)

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“…Although the yield of (2 S ,3 S )-2,3-BD was not very high due to the low content of (2 S ,3 S )-2,3-BD in the mixture of 2,3-BD (only 12.4%), the biocatalytic efficiency of the (2 R ,3 R )-2,3-BDH and NOX coexpressing recombinant strain was much higher than that of recombinant E. coli expressing GDH only (1.4 g L −1 ) [20]. This shows that the incorporation of a cofactor regeneration system in the E. coli whole-cell biocatalyst is a powerful strategy for enhancing the catalytic efficiency of oxidoreductases.…”

Section: Resultsmentioning

confidence: 94%

A Novel Whole-Cell Biocatalyst with NAD+ Regeneration for Production of Chiral Chemicals

et al. 2010

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BackgroundThe 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.Methodology/Principal FindingsSimultaneous overexpression of an NAD+ dependent enzyme and an NAD+ regenerating enzyme (H2O 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.Conclusions/SignificanceA 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.

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Section: Resultsmentioning

confidence: 94%

A Novel Whole-Cell Biocatalyst with NAD+ Regeneration for Production of Chiral Chemicals

et al. 2010

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“…Moreover, several glycerol dehydrogenases (GDHs) also catalyzed the oxidation of (2R,3R)-2,3-BD into (3R)-AC when NAD + was used as a cofactor [19][20][21][22]. Yamada-Onodera et al [23] developed a recombinant E. coli expressing the GDH enzyme of Hansenula polymorpha Dl-1 for the bioconversion of (2R,3R)-2,3-BD into (3R)-AC. However, (3R)-AC with a low yield of 9.68 g/l was produced by the recombinant strain without other additives to regenerate NAD + from NADH [23].…”

Section: Introductionmentioning

confidence: 99%

Efficient (3R)-Acetoin Production from meso-2,3-Butanediol Using a New Whole-Cell Biocatalyst with Co-Expression of meso-2,3-Butanediol Dehydrogenase, NADH Oxidase, and Vitreoscilla Hemoglobin

Guo¹,

Zhao²,

He³

et al. 2017

Journal of Microbiology and Biotechnology

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Acetoin (AC) is a volatile platform compound with various potential industrial applications. AC contains two stereoisomeric forms: (3)-AC and (3)-AC. Optically pure AC is an important potential intermediate and widely used as a precursor to synthesize novel optically active materials. In this study, chiral (3)-AC production from -2,3-butanediol (-2,3-BD) was obtained using recombinant cells co-expressing-2,3-butanediol dehydrogenase (-2,3-BDH), NADH oxidase (NOX), and hemoglobin protein (VHB) from sp. T241,, and , respectively. The new biocatalyst of/pET--- was developed and the bioconversion conditions were optimized. Under the optimal conditions, 86.74 g/l of (3)-AC with the productivity of 3.61 g/l/h and the stereoisomeric purity of 97.89% was achieved from 93.73 g/l -2,3-BD using the whole-cell biocatalyst. The yield and productivity were new records for (3)-AC production. The results exhibit the industrial potential for (3)-AC production via whole-cell biocatalysis.

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“…As such, we presently remain unable to comment on the identity and activity of these specific gene products. It is worth noting that 2,3-BD dehydrogenase activity has previously been demonstrated by glycerol dehydrogenase of the yeast Hansenula polymorpha (Pichia angusta) [29,30]. Whereas E. coli also possesses a glycerol dehydrogenase (encoded by gldA), its substrate specificity with respect to the reduction of acetoin to meso-2,3-BD has not yet been examined.…”

Section: Resultsmentioning

confidence: 99%

Metabolic engineering of acetoin and meso‐2, 3‐butanediol biosynthesis in E. coli

Nielsen

Yoon

Yuan

et al. 2010

Biotechnology Journal

108

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The functional reconstruction of acetoin and meso-2,3-butanediol (meso-2,3-BD) biosynthetic pathways in Escherichia coli have been explored systematically. Pathway construction involved the in vivo screening of prospective pathway isozymes of yeast and bacterial origin. After substantial engineering of the host background to increase pyruvate availability, E. coli YYC202(DE3) ldhA − ilvC − expressing ilvBN from E. coli and aldB from L. lactis (encoding acetolactate synthase and acetolactate decarboxylase activities, respectively) was able to produce up to 870 mg/L acetoin, with no coproduction of diacetyl observed. These strains were also found to produce small quantities of meso-2,3-BD, suggesting the existence of endogenous 2,3-BD dehydrogenase activity. Finally, the coexpression of bdh1 from S. cerevisiae, encoding 2,3-BD dehydrogenase, in this strain resulted in the production of up to 1120 mg/L meso-2,3-BD, with glucose a yield of 0.29 g/g. While disruption of the native lactate biosynthesis pathway increased pyruvate precursor availability to this strain, increased availability of NADH for acetoin reduction to meso-2,3-BD was found to be the most important consequence of ldhA deletion.

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Expression of the Gene of Glycerol Dehydrogenase from Hansenula polymorpha Dl-1 in Escherichia coli for the Production of Chiral Compounds

Cited by 25 publications

References 0 publications

A Novel Whole-Cell Biocatalyst with NAD+ Regeneration for Production of Chiral Chemicals

A Novel Whole-Cell Biocatalyst with NAD+ Regeneration for Production of Chiral Chemicals

Efficient (3R)-Acetoin Production from meso-2,3-Butanediol Using a New Whole-Cell Biocatalyst with Co-Expression of meso-2,3-Butanediol Dehydrogenase, NADH Oxidase, and Vitreoscilla Hemoglobin

Metabolic engineering of acetoin and meso‐2, 3‐butanediol biosynthesis in E. coli

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