| Abstract: | The mosquito-parasitizing fungus Lagenidium giganteum secreted a soluble acid phosphatase and beta-D-glucosidase into the growth medium. The acid phosphatase was isolated and purified to single component, and some of its physicochemical properties were determined. The enzyme exhibited a pH optimum of 5.6 in phthalate buffer with p-nitrophenyl phosphate and was temperature-inactivated at 55 degrees C. Enzyme activity seems to be limited to phenyl-phosphate substrates. A molecular weight of 42,800 was found and the amino acid content was also determined. A Km for p-nitrophenyl phosphate of 1.6 x 10(-7) M was found. The possible involvement of the enzyme in the infective process was discussed. |
