Purification and characterization of alkaline phosphatase from lactic acid bacteria
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Abstract
Alkaline phosphatase (ALP) excreted from lactic acid bacteria (LAB) showed the ability to degrade organophosphorus pesticides. This study reported the first purification and characterization of ALP from LAB. The molecular weight of ALP was estimated to be 43 kDa measured by SDS-PAGE. The activity of purified enzyme was determined with the binding of p-nitrophenyl phosphate as the substrate. The results showed that the optimal temperature for ALP activity was 37 °C, and the optimal pH was 8.5. But ALP was stable at temperatures below 32 °C. The ALP activity remained at 80% when the pH was 8–9.5. The enzyme activity could be activated by Mg2+, Ca2+, and inhibited by Cu2+, Zn2+, and EDTA. The Michaelis–Menten constant was 6.05 mg kg−1 with dimethoate as the substrate according to the Lineweaver–Burk plots. These results highlight an important potential use of ALP from LAB for the cleanup of pesticide pollution in raw materials for the food industry.
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