A novel enzymatic approach to the massproduction of L-galactose from L-sorbose

Leang, Khim; Maekawa, Kanako; Menavuvu, Buetusiwa Thomas; Morimoto, Kenji; Granström, Tom; Takada, Goro; Izumori, Ken

doi:10.1016/s1389-1723(04)70223-6

Cited by 32 publications

(12 citation statements)

References 36 publications

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“…L-Sorbose is recognized as a suitable intermediate in the industrial manufacturing of value-added chemicals such as vitamin C, 1-deoxygalactonojirimycin, and L-tagatose 1 2 3 4 . Bacterial fermentation has become the sole method for L-sorbose production 31 .…”

Section: Resultsmentioning

confidence: 99%

“…L-Sorbose is a unique sugar that is used extensively as a primary precursor for the biosynthesis of L-ascorbic acid in a two-step fermentation of D-sorbitol to L-sorbose and L-sorbose to 2-keto- l -gulonic acid 1 2 . 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 .…”

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confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

mentioning

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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“…l -Sorbose is largely used as a starting material for l -ascorbic acid biosynthesis 4,5 . It has been also used to synthesize the potent glycosidase inhibitor 1-deoxygalactonojirim 6 and rare sugars such as l -tagatose 7 and l -iditol 8 .…”

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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“…Leang et al established an efficient two-step method for synthesizing L-galactose on a large scale from a common sugar L-sorbose, catalyzed by immobilized DTEase from a mutant Pseudomonas sp. ST-24 and recombinant L-rhamnose isomerase from Escherichia coli JM109 [88]. L-Sorbose was first epimerized by DTEase at C-3 to give L-tagatose (28% yield), which reached an equilibrium with L-galactose (~30%) catalyzed by the L-rhamnose isomerase (Scheme 15).…”

Section: Reviewmentioning

confidence: 99%

Biosynthesis of rare hexoses using microorganisms and related enzymes

Li¹,

Gao²,

Nakanishi³

et al. 2013

Beilstein J. Org. Chem.

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SummaryRare sugars, referred to as monosaccharides and their derivatives that rarely exist in nature, can be applied in many areas ranging from foodstuffs to pharmaceutical and nutrition industry, or as starting materials for various natural products and drug candidates. Unfortunately, an important factor restricting the utilization of rare sugars is their limited availability, resulting from limited synthetic methods. Nowadays, microbial and enzymatic transformations have become a very powerful tool in this field. This article reviews the biosynthesis and enzymatic production of rare ketohexoses, aldohexoses and sugar alcohols (hexitols), including D-tagatose, D-psicose, D-sorbose, L-tagatose, L-fructose, 1-deoxy-L-fructose, D-allose, L-glucose, L-talose, D-gulose, L-galactose, L-fucose, allitol, D-talitol, and L-sorbitol. New systems and robust catalysts resulting from advancements in genomics and bioengineering are also discussed.

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A novel enzymatic approach to the massproduction of L-galactose from L-sorbose

Cited by 32 publications

References 36 publications

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

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

Biosynthesis of rare hexoses using microorganisms and related enzymes

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