Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/53190
Type: Artigo de periódico
Title: A fluorescence-based assay for Baeyer-Villiger monooxygenases, hydroxylases and lactonases
Author: Sicard, R
Chen, LS
Marsaioli, AJ
Reymond, JL
Abstract: Alkylation of umbelliferone and nitrophenol with chloroacetone, 3-chlorobutanone, 2-chlorocyclopentanone and 2-chlorocyclohexanone gave the corresponding 2-coumaryloxy and 2-nitrophenoxy ketones. The 2-coumarytoxy ketones were used as fluorogenic substrates to detect Baeyer-Villiger monooxygenases activities of microbial cultures in high-throughput using microtiter plates. The 2-coumaryloxy ketones were oxidized by microorganisms producing Baeyer-Villiger monooxygenases (BVMO), releasing umbelliferone as a fluorescent signal. The substrates were also biotransformed by a microbial monooxygenase (Trichosporon cutaneum). Chemical Baeyer-Villiger oxidation of 2-coumaryloxy ketones using meta-chloroperbenzoic acid proceeded regioselectively to the corresponding acyloxyalkyl derivatives of umbelliferone and nitrophenol. These chiral lactones underwent a fluorogenic and chromogenic reaction upon hydrolysis by esterases, in particular pig liver esterase. Enantioselectivity of the ester hydrolysis reaction was determined by chiral-phase analysis of the unreacted lactones.
Subject: biotransformations
enzyme catalysis
fluorescent probes
lactones
oxidation
Country: EUA
Editor: Wiley-blackwell
Rights: fechado
Identifier DOI: 10.1002/adsc.200505040
Date Issue: 2005
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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