IQUIR   05412
INSTITUTO DE QUIMICA ROSARIO
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
A novel Baeyer-Villiger monooxygenase as biocatalyst
Autor/es:
CECCOLI, ROMINA D.; BIANCHI, DARIO A.; RIAL, DANIELA V.
Lugar:
Rosario
Reunión:
Congreso; L Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2014
Institución organizadora:
Sociedad Argentina de Investigación Bioquímica y Biología Molecular
Resumen:
The Baeyer-Villiger oxidation of ketones to produce esters or lactones is a valuable synthetic reaction for the preparation of building blocks, pharmaceutical intermediates, bioactive compounds and natural products. The use of enzymes as catalysts takes advantage of the selectivity, efficiency and mild conditions of enzyme-mediated reactions. Type I Baeyer-Villiger monooxygenases (BVMOs) are FAD-dependent enzymes that catalyze the insertion of one atom from molecular oxygen into the substrate, whereas the other atom is reduced to water at the expense of NADPH. The aim of this work was to characterize a novel BVMO in order to expand the number of biocatalysts available for chemical applications. We identified a putative BVMO from Leptospira biflexa (Paris) proteome and found that this flavoprotein is distantly related to the main groups of previously characterized BVMOs according to phylogenetic analysis. Besides, its structure was predicted by homology modelling compared to published BVMO structures. We studied the substrate preference profile of this BVMO by biotransformations in recombinant whole-cell systems (growing and/or resting cells) with different ketones as substrates. Our results indicate that the BVMO from L. biflexa is able to oxidize linear short-chain ketones as well as some cyclic and aromatic compounds.