Extracellular pH 2.5 Optimum Acid Phosphatase fromAspergillus Ficuum: Immobilization On Modified Fractogel

Abstract
Aspergillus ficuum pH 2.5 optimum acid phosphatase (orthophosphoric monoesters phosphohydrolase, E. C. 3.1.3.2) was covalently immbolized 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 K1 for orthophosphate was changed from 185 μM to 422 μM and greater stability was observed against heat treatment.