Utilize este identificador para referenciar este registo: http://hdl.handle.net/10451/21644
Título: Kinetic properties of glycerophosphate oxidase isolated from dry baker's yeast
Autor: Camargo, Luciana Amade
Lourenco Ribeiro, Maria Henriques
Sanches Peres, Maristela de Freitas
de Lucca Gattas, Edwil Aparecida
Data: 2008
Editora: ELSEVIER SCIENCE BV
Citação: JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC. - Vol. 52-3 (JUN 2008), p. 140-145
Resumo: The glycerophosphate oxidase is a flavoprotein responsible for the catalysis of the oxidation of the glycerophosphate to dihydroxyacetone phosphate, through the reduction of the oxygen to hydrogen peroxide. The glycerophosphate oxidase from baker's yeast was specific for L-alpha-glycerol phosphate. It was estimated by monitoring the consumption of oxygen with an oxygraph. An increase of 32% in consumption of oxygen was obtained when the enzyme was concentrated 16-fold. The assay of enzyme was determined by the peroxidase chromogen method followed at 500 nm. The procedure for the standardization of the activity of the glycerophosphate oxidase from baker's yeast was accomplished, and the pH and temperature stability showed that the enzyme presented a high stability at pH 8.0, and the thermal stability was maintained up to 60 degrees C during I h. Such method allowed quantifying in the range 92-230 mM of glycerol phosphate, an important intermediate metabolite from lipid biosynthesis and glycolytic routes. (C) 2007 Elsevier B.V. All rights reserved.
URI: http://hdl.handle.net/10451/21644
DOI: http://dx.doi.org/10.1016/j.molcatb.2007.11.011
ISSN: 1381-1177
Aparece nas colecções:FF - Produção Científica 2000-2009

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