Lignin peroxidase dephosphorylating phosphatase from Phanerochaete chrysosporium

Nathan Rothschild*, Ayala Levkowitz, Yitzhak Hadar, Carlos Dosoretz

*Corresponding author for this work

Research output: Contribution to conferencePaperpeer-review

1 Scopus citations

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 languageEnglish
PagesB77-B79
StatePublished - 1998
Externally publishedYes
EventProceedings of the 1998 7th International Conference on Biotechnology in the Pulp and Paper Industry. Part 1 (of 3) - Vancouver, Can
Duration: 16 Jun 199819 Jun 1998

Conference

ConferenceProceedings of the 1998 7th International Conference on Biotechnology in the Pulp and Paper Industry. Part 1 (of 3)
CityVancouver, Can
Period16/06/9819/06/98

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