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Single-enzyme redox-neutral oxidation of alcohols to carboxylic acids using alcohol dehydrogenases.


ABSTRACT: Oxidation of primary alcohols to carboxylic acids is a fundamental reaction in organic chemistry, traditionally dependent on toxic oxidants and often limited by poor selectivity. In this study, we demonstrate the multifunctional capability of some alcohol dehydrogenases (ADHs) to catalyze both alcohol and aldehyde oxidation while regenerating their NAD+ cofactor through concomitant reduction of acetone. Screening of a panel of ADHs revealed that the enzymes from Paracoccus pantotrophus (Pp-ADH) and Aromatoleum aromaticum (Aa-ADH) have strong overoxidation activity to carboxylic acids. The biocatalytic method was assessed for the efficient oxidation of a panel of 27 structurally diverse primary alcohols into carboxylic acids using a single enzyme, with

SUBMITTER: Damian M 

PROVIDER: S-EPMC12775759 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature

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Single-enzyme redox-neutral oxidation of alcohols to carboxylic acids using alcohol dehydrogenases.

Damian Matteo M   Wei Zheng Z   Tseliou Vasilis V   Mutti Francesco G FG  

Catalysis science & technology 20251210 3


Oxidation of primary alcohols to carboxylic acids is a fundamental reaction in organic chemistry, traditionally dependent on toxic oxidants and often limited by poor selectivity. In this study, we demonstrate the multifunctional capability of some alcohol dehydrogenases (ADHs) to catalyze both alcohol and aldehyde oxidation while regenerating their NAD<sup>+</sup> cofactor through concomitant reduction of acetone. Screening of a panel of ADHs revealed that the enzymes from <i>Paracoccus pantotro  ...[more]

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