By-product formation in the d-sorbitol to l-sorbose biotransformation by Gluconobacter suboxydans ATCC 621 in batch and continuous cultures

Macauley-Patrick, Sue; McNeil, Brian; Harvey, Linda M.

doi:10.1016/j.procbio.2004.07.014

Cited by 13 publications

(9 citation statements)

References 30 publications

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“…L-sorbose is an important carbohydrate that is predominantly used as a starting material in the biosynthesis of L-ascorbic acid [ 1 , 2 ]. The most prominent industrial method of producing L-sorbose is the biotransformation of D-sorbitol to L-sorbose in Gluconobacter species or Acetobacter species [ 3 , 4 ]. During the process, two hydrogen atoms were removed from one molecular of D-sorbitol to form one molecular of L-sorbose.…”

Section: Introductionmentioning

confidence: 99%

Enhanced production of L-sorbose from D-sorbitol by improving the mRNA abundance of sorbitol dehydrogenase in Gluconobacter oxydansWSH-003

Wang

et al. 2014

Microb Cell Fact

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BackgroundProduction of L-sorbose from D-sorbitol by Gluconobacter oxydans is the first step to produce L-ascorbic acid on industrial scale. The sldhAB gene, which encodes the sorbitol dehydrogenase (SLDH), was overexpressed in an industrial strain G. oxydans WSH-003 with a strong promoter, PtufB. To enhance the mRNA abundance, a series of artificial poly(A/T) tails were added to the 3′-terminal of sldhAB gene. Besides, their role in sldhAB overexpression and their subsequent effects on L-sorbose production were investigated.ResultsThe mRNA abundance of the sldhAB gene could be enhanced in G. oxydans by suitable poly(A/T) tails. By self-overexpressing the sldhAB gene in G. oxydans WSH-003 with an optimal poly(A/T) tail under the constitutive promoter PtufB, the titer and the productivity of L-sorbose were enhanced by 36.3% and 25.0%, respectively, in a 1-L fermenter. Immobilization of G. oxydans-sldhAB6 cells further improved the L-sorbose titer by 33.7% after 20 days of semi-continuous fed-batch fermentation.ConclusionsThe artificial poly(A/T) tails could significantly enhance the mRNA abundance of the sldhAB. Immobilized G. oxydans-sldhAB6 cells could further enlarge the positive effect caused by enhanced mRNA abundance of the sldhAB.

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Section: Introductionmentioning

confidence: 99%

Enhanced production of L-sorbose from D-sorbitol by improving the mRNA abundance of sorbitol dehydrogenase in Gluconobacter oxydansWSH-003

Wang

et al. 2014

Microb Cell Fact

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“…It is used in the synthesis of 1-deoxygalactonojirimycin, a glycosidase inhibitor 3 , and as a starting material for producing L-tagatose 4 . Gluconobacter and Acetobacter are well known for the effective conversion of D-sorbitol into L-sorbose through regio-controlled D-sorbitol dehydrogenation 5 6 . G. oxydans is preferred in the production of L-sorbose from D-sorbitol via biotransformation.…”

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confidence: 99%

A highly efficient sorbitol dehydrogenase from Gluconobacter oxydans G624 and improvement of its stability through immobilization

Kim

Patel

Selvaraj

et al. 2016

Sci Rep

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A sorbitol dehydrogenase (GoSLDH) from Gluconobacter oxydans G624 (G. oxydans G624) was expressed in Escherichia coli BL21(DE3)-CodonPlus RIL. The complete 1455-bp codon-optimized gene was amplified, expressed, and thoroughly characterized for the first time. GoSLDH exhibited Km and kcat values of 38.9 mM and 3820 s−1 toward L-sorbitol, respectively. The enzyme exhibited high preference for NADP+ (vs. only 2.5% relative activity with NAD+). GoSLDH sequencing, structure analyses, and biochemical studies, suggested that it belongs to the NADP+-dependent polyol-specific long-chain sorbitol dehydrogenase family. GoSLDH is the first fully characterized SLDH to date, and it is distinguished from other L-sorbose-producing enzymes by its high activity and substrate specificity. Isothermal titration calorimetry showed that the protein binds more strongly to D-sorbitol than other L-sorbose-producing enzymes, and substrate docking analysis confirmed a higher turnover rate. The high oxidation potential of GoSLDH for D-sorbitol was confirmed by cyclovoltametric analysis. Further, stability of GoSLDH significantly improved (up to 13.6-fold) after cross-linking of immobilized enzyme on silica nanoparticles and retained 62.8% residual activity after 10 cycles of reuse. Therefore, immobilized GoSLDH may be useful for L-sorbose production from D-sorbitol.

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“…The most widely used industrial method for producing l -sorbose is the biotransformation of d- sorbitol to l -sorbose using Gluconobacter or Acetobacter species 15,16 . In our previous study, GoSLDH showed the higher activity towards d- sorbitol compared to other polyol dehydrogenases 17 .…”

Section: Introductionmentioning

confidence: 99%

Overcoming NADPH product inhibition improves D-sorbitol conversion to L-sorbose

Kim

Gao

et al. 2019

Sci Rep

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Gluconobacter oxydans sorbitol dehydrogenase (GoSLDH) exhibits a higher catalytic efficiency than other l-sorbose producing enzymes. During the reaction catalysed by GoSLDH, NADP+ is reduced to NADPH and d-sorbitol is oxidized to l-sorbose. However, GoSLDH activity is inhibited by the NADPH (Ki = 100 μM) formed during the enzymatic reaction. Therefore, Escherichia coligosldh-lrenox producing both GoSLDH for d-sorbitol oxidation and LreNOX (NAD(P)H oxidase from Lactobacillus reuteri) for NADP+ regeneration was generated and used for l-sorbose production. Whole cell biocatalysts with the LreNOX cofactor recycling system showed a high conversion rate (92%) of d-sorbitol to l-sorbose in the presence of low concentration of NADP+ (0.5 mM). By alleviating NADPH accumulation during the catalytic reactions, E. coligosldh-lrenox exhibited 23-fold higher conversion rate of d-sorbitol than E. coligosldh. l-Sorbose production by E. coligosldh-lrenox reached 4.1 g/L after 40 min, which was 20.5-fold higher than that of E. coligosldh. We also constructed G. oxydansgosldh and G. oxydansgosldh-lrenox strains, and they exhibited 1.2- and 2.9-fold higher conversion rates than the wild-type G. oxydans KCTC 1091. The results indicate that overcoming NADPH product inhibition using LreNOX improves chemical production in NADP+-dependent enzymatic reactions.

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By-product formation in the d-sorbitol to l-sorbose biotransformation by Gluconobacter suboxydans ATCC 621 in batch and continuous cultures

Cited by 13 publications

References 30 publications

Enhanced production of L-sorbose from D-sorbitol by improving the mRNA abundance of sorbitol dehydrogenase in Gluconobacter oxydansWSH-003

Enhanced production of L-sorbose from D-sorbitol by improving the mRNA abundance of sorbitol dehydrogenase in Gluconobacter oxydansWSH-003

A highly efficient sorbitol dehydrogenase from Gluconobacter oxydans G624 and improvement of its stability through immobilization

Overcoming NADPH product inhibition improves D-sorbitol conversion to L-sorbose

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