Article Purification and Characterization of Alkaline Phosphatase from Pleurotus sajor-caju

Antik K. Bose

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Biochemical properties of alkaline phosphatase obtained from fruiting body extract of Pleurotus sajor-caju were described. The enzyme was purified 27117.64 fold with 9.6% recovery by DEAE-cellulose and Sephadex G-200 Chromatography. The molar mass estimated by Sephadex G-200 was 130KD and 6% SDS-PAGE, two subunits of molecular mass 89.8KD and 42.5KD were obtained indicating a heterodimer. Temperatur C and pH 8.5 respectively. The enzyme was moderately glycosylated ( 44% saccharide 2+ 2+ content ). The activity was enhanced by Mg (7-96.8%), Mn (17-48%), + Na (2.46-14.28%). 4-nitrophenyl phosphate was hydrolysed with KM and Vmax of 25mM-1 and 0.285M of PNPP consumed/min respectively. Amino acids at the active site have been identified using Diisopropylphosphofloridate (DIPF), Diethylpyrocarbonate (DEPC), Diazomethane and 1-ethyl-3( 3-dimethyl) aminopropyl carbodiimide (EDAC) to be serine, histidine and aspartic acid respectively.

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