Title of article :
Kinetic properties of glycerophosphate oxidase isolated from dry bakerʹs yeast
Author/Authors :
Camargo، نويسنده , , Luciana Amade and Ribeiro، نويسنده , , Maria Henriques Lourenço and de Freitas Sanches Peres، نويسنده , , Maristela and Gattلs، نويسنده , , Edwil Aparecida de Lucca، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2008
Pages :
6
From page :
140
To page :
145
Abstract :
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 bakerʹs 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 bakerʹs 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.
Keywords :
Bakerיs yeast , Glycerophosphate oxidase , kinetic properties
Journal title :
Journal of Molecular Catalysis B Enzymatic
Serial Year :
2008
Journal title :
Journal of Molecular Catalysis B Enzymatic
Record number :
1716599
Link To Document :
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