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Purification and characterization of a β-1,4-endoxylanase from the ericoid mycorrhizal fungus <em>Hymenoscyphus ericae</em>.
- Source :
- New Phytologist; Feb97, Vol. 135 Issue 2, p345-352, 8p
- Publication Year :
- 1997
-
Abstract
- A β-1,4-endoxylanase from the ericoid mycorrhizal fungus <em>H. ericae</em> has been purified to electrophoretic homogeneity using isoelectric focusing, ion exchange and gel permeation chromatography. The enzyme has an isoelectric point of 4.85-5.2O and a molecular weight of 58.4 kDa. The apparent S<subscript>0.5</subscript> of the enzyme for soluble birchwood glucuronoxylan is 3.75 mg ml<superscript>-1</superscript> and the <em>V</em><subscript>max</subscript> 468.0 nkatal mg<superscript>-1</superscript> protein. The pH optimum for activity is 4.5 and that for stability is 3.5-4.0; these values are discussed in the context of the pH of the mor humus. The role of wall-degrading activities in the establishment of the ericoid mycorrhizal symbiosis is considered. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 0028646X
- Volume :
- 135
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- New Phytologist
- Publication Type :
- Academic Journal
- Accession number :
- 12500019
- Full Text :
- https://doi.org/10.1046/j.1469-8137.1997.00634.x