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


ABSTRACT: 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??M) 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.

SUBMITTER: Kim TS 

PROVIDER: S-EPMC6349845 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature

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

Kim Tae-Su TS   Gao Hui H   Li Jinglin J   Kalia Vipin C VC   Muthusamy Karthikeyan K   Sohng Jae Kyung JK   Kim In-Won IW   Lee Jung-Kul JK  

Scientific reports 20190128 1


Gluconobacter oxydans sorbitol dehydrogenase (GoSLDH) exhibits a higher catalytic efficiency than other L-sorbose producing enzymes. During the reaction catalysed by GoSLDH, NADP<sup>+</sup> is reduced to NADPH and D-sorbitol is oxidized to L-sorbose. However, GoSLDH activity is inhibited by the NADPH (K<sub>i</sub> = 100 μM) formed during the enzymatic reaction. Therefore, Escherichia coli<sub>gosldh-lrenox</sub> producing both GoSLDH for D-sorbitol oxidation and LreNOX (NAD(P)H oxidase from La  ...[more]

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