Kinetic properties of glycerophosphate oxidase isolated from dry baker's yeast

Kinetic properties of glycerophosphate oxidase isolated from dry baker's yeast

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-α-glycerol phosphate....

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Bibliographic Details
Published in:Journal of molecular catalysis. B, Enzymatic Vol. 52; pp. 140 - 145
Main Authors: Camargo, Luciana Amade, Ribeiro, Maria Henriques Lourenço, de Freitas Sanches Peres, Maristela, Gattás, Edwil Aparecida de Lucca
Format: Journal Article Conference Proceeding
Language:English
Published: Amsterdam Elsevier B.V 01-06-2008
Elsevier Science
Subjects:
Baker's yeast
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Fundamental and applied biological sciences. Psychology
Glycerophosphate oxidase
Kinetic properties
Methods. Procedures. Technologies
Baker's yeast
Glycerophosphate oxidase
Kinetic properties
Enzyme
Substrate specificity
Baker yeast
Oxidoreductases
Kinetics
Physicochemical properties
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Summary: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-α-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 °C during 1 h. Such method allowed quantifying in the range 92–230 mM of glycerol phosphate, an important intermediate metabolite from lipid biosynthesis and glycolytic routes.
ISSN:1381-1177
1873-3158
DOI:10.1016/j.molcatb.2007.11.011