Extracellular PH 2.5 optimum acid phosphatase from Aspergillus ficuum: immobilization on modified fractogel.
Aspergillus ficuum pH 2.5 optimum acid phosphatase (orthophosphoric monoesters phosphohydrolase, E.C.3.1.3.2) was covalently immobolized on 2-fluoro-1-methylpyridinium toluene-4-sulfonate (FMP)-activated Fractogel TSK HW-50F. The catalytic parameters and stability of the immobilized enzyme were compared with those of the free enzyme. While the Km and the temperature optima were unchanged, the Ki for orthophosphate was changed from 185 microM to 422 microM and greater stability was observed against heat treatment.
Ullah
A H
AH
Southern Regional Research Laboratory ARS, USDA, New Orleans, Louisiana 70124.
Cummins
B J
BJ
D000135:Acid Phosphatase / Q000302:isolation & purification* / Q000378:metabolism; D001230:Aspergillus / Q000201:enzymology*; D004800:Enzymes, Immobilized / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D013696:Temperature
D004800:Enzymes, Immobilized; D000135:Acid Phosphatase