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Enzymatic production of atranorin: a component of the oak moss absolute by immobilized lichen cells
Author(s) -
Vicente C.,
Fontaniella B.,
Millanes A. M.,
Sebastián B.,
Legaz M. E.
Publication year - 2003
Publication title -
international journal of cosmetic science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.532
H-Index - 62
eISSN - 1468-2494
pISSN - 0142-5463
DOI - 10.1046/j.1467-2494.2003.00169.x
Subject(s) - sodium azide , alcohol dehydrogenase , chemistry , enzyme , dehydrogenase , biochemistry , aldehyde , azide , alcohol , calcium alginate , aldehyde dehydrogenase , nuclear chemistry , stereochemistry , organic chemistry , calcium , catalysis
Synopsis Cells of the lichen, Evernia prunastri , immobilized in calcium alginate were able to produce the depside atranorin from acetate. The synthesis of the depside was enhanced by molecular oxygen and NADH. This enhancement suggested the participation of an oxidase and an alcohol dehydrogenase to produce an aldehyde‐substituted phenolic acid, hematommic acid, as the most probable precursor of atranorin. The participation of both enzymes was confirmed by loading immobilized cells with sodium azide, an inhibitor of several metallo‐oxidases, and pyrazole, an inhibitor of alcohol dehydrogenase, which impeded atranorin production and accumulated β‐methyl orsellinate (after azide loading) or its alcohol derivative (after pirazole treatment).