Lignin peroxidase dephosphory-lating phosphatase from phanerochanete chrysosporium.

摘要

A phosphatase from extracellular culture fluid filtrate of the fungus Phanerochaete chrysosporium was partly purified. Incubation of the phsophatse with lignin peroxidase isozyme H2 resulted in its complete conversion to isozyme H2 resulted in tis complete conversion to siozyme Hi, with an equimolar reloease of phsophate. The phosphatase exhibited narrow specificity with sugar phosphates as substrate, showing activity mostly for mannose-6-phosphate. Phosphatase activity was inhibited by EDTA, vanadate or molybdate, enhanced 2.5 fold by manganese or cobalt salts and was optimal at pH 5.