This review discusses how cofactor regeneration using nadph oxidase improves production of value-added chemicals, highlighting its role in enzymatic production and biotransformations.
Nicotinamide adenine dinucleotide (phosphate) oxidases are the enzymes that catalyze the oxidation of NAD(P)H to produce NAD(P) + , which is the cofactor of many dehydrogenases. To reduce costs, cofactor regeneration of NAD(P)+ is essential for both enzymatic and whole-cell biotransformations. In the present review, the enzymatic or microbial production of rare sugars like L-tagatose, L-xylulose, L-gulose, and L-sorbose with cofactor regeneration was summarized. And the cofactor regeneration in some value-added chemicals, including acetoin, 1,3-dihydroacetone, vanillic acid, chlorolactone, acetophenone, and kinetic resolution of racemic phenylethanol by employing NADH/NADPH oxidase was also reviewed. The engineering of these enzymes by modifying the enzyme surface, reshaping the catalytic pocket, and mutating the substrate-binding domain of NADH oxidase to improve the catalytic performance for potential industrial applications was discussed in the future outlook.
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Zhou et al. (2025) studied this question.
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