Uncommon overoxidative catalytic activity in a new halo‐tolerant alcohol dehydrogenase

Contente, Martina L.; Fiore, Noemi; Cannazza, Pietro; Roura Padrosa, David; Molinari, Francesco; Gourlay, Louise; Paradisi, Francesca (2020). Uncommon overoxidative catalytic activity in a new halo‐tolerant alcohol dehydrogenase. ChemCatChem, 12(22), pp. 5679-5685. WILEY-VCH 10.1002/cctc.202001112

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Alcohol dehydrogenases (ADH) are versatile and useful enzymes employed as biocatalysts, especially for the selective oxidation of primary and secondary alcohols, and for the reduction of carbonyl moieties. A new alcohol dehydrogenase (HeADH‐II) has been identified from the genome of the halo‐adapted bacterium Halomonas elongata, which proved stable in the presence of polar organic solvents and salt exposure. Unusual for this class of enzymes, HeADH‐II lacks enantiopreference and is capable of oxidizing both alcohols and aldehydes, enabling a direct overoxidation of primary alcohols to carboxylic acids. HeADH‐II was coupled with a NADH‐oxidase from Lactobacillus pentosus (LpNOX) to increase the process yields and allowing recycling of the cofactor. The enzymatic oxidation of primary alcohols was also paired with in situ condensation of the intermediate aldehydes with hydroxylamine to prepare the corresponding aldoximes, with particular attention to perillartine (a powerful sweetener), whose enzymatic synthesis starting from natural sources, leads to an equally natural product.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP)

UniBE Contributor:

Contente, Martina Letizia; Roura Padrosa, David and Paradisi, Francesca

Subjects:

500 Science > 540 Chemistry

ISSN:

1867-3880

Publisher:

WILEY-VCH

Funders:

[164] Marie Skłodowska-Curie actions

Language:

English

Submitter:

Francesca Paradisi

Date Deposited:

14 Sep 2020 08:33

Last Modified:

19 Aug 2021 02:30

Publisher DOI:

10.1002/cctc.202001112

BORIS DOI:

10.7892/boris.146504

URI:

https://boris.unibe.ch/id/eprint/146504

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