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Uncommon overoxidative catalytic activity in a new halo‐tolerant alcohol dehydrogenase
Author(s) -
Contente Martina L.,
Fiore Noemi,
Cannazza Pietro,
Roura Padrosa David,
Molinari Francesco,
Gourlay Louise,
Paradisi Francesca
Publication year - 2020
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.202001112
Subject(s) - chemistry , alcohol dehydrogenase , alcohol oxidation , alcohol , organic chemistry , catalysis , hydroxylamine , primary (astronomy) , cofactor , formate dehydrogenase , combinatorial chemistry , primary alcohol , enzyme , physics , astronomy
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 ( Lp NOX) 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.