Abstract
A phosphatase from extracellular culture fluid filtrate of the fungus Phanerochaete chrysosporium was partly purified. Incubation of the phosphatase with lignin peroxidase isozyme H2 resulted in its complete conversion to isozyme H1, with an equimolar release of phosphate. 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.
Original language | English |
---|---|
Pages | B77-B79 |
State | Published - 1998 |
Externally published | Yes |
Event | Proceedings of the 1998 7th International Conference on Biotechnology in the Pulp and Paper Industry. Part 1 (of 3) - Vancouver, Can Duration: 16 Jun 1998 → 19 Jun 1998 |
Conference
Conference | Proceedings of the 1998 7th International Conference on Biotechnology in the Pulp and Paper Industry. Part 1 (of 3) |
---|---|
City | Vancouver, Can |
Period | 16/06/98 → 19/06/98 |