Purification and biochemical characterization of a mycelial alkaline phosphatase without DNAase activity produced byAspergillus caespitosus

Biochemical properties of a termostable alkaline phosphatase obtained from the mycelium extract ofA. caespitosus were described. The enzyme was purified 42-fold with 32 % recovery by DEAE-cellulose and concanavalin A-Sepharose chromatography. The molar mass estimated by Sephacryl S-200 or by 7 % SDS-PAGE was 138 kDa and 71 kDa, respectively, indicating a… CONTINUE READING