Purification and enzymatic characterization of alkaline phosphatase from Pinctada fucata

An alkaline phosphatase was purified from Pinctada fucata, a kind of pearl oyster, by chromatography on DEAE-32 cellulose, Sephadex G-150 and DEAE A-25. The specific activity of the enzyme was 2040 U mg−1. The kinetics characteristics of the enzyme have been studied. The product HPO42− and the product-analog WO43− competitively inhibited the enzyme activity. Positive monovalent cations had no effect on the enzyme activity, while positive bivalent cations had different effects on the enzyme: Mg2+, Ca2+, Co2+ and Mn2+ activated the enzyme while Zn2+, Cu2+ and Cd2+ inhibited the enzyme.