Hostname: page-component-586b7cd67f-dlnhk Total loading time: 0 Render date: 2024-11-24T09:50:03.946Z Has data issue: false hasContentIssue false
  • English
  • Français

Purification and characterization of a β-1,4-endoxylanase from the ericoid mycorrhizal fungus Hymenoscyphus ericae

Published online by Cambridge University Press:  01 February 1997

R. M. BURKE  and
J. W. G. CAIRNEY
R. M. BURKE
Affiliation:
Department of Biochemistry and Applied Molecular Biology, UMIST, P.O. Box 88, Manchester M60 1QD, UK
J. W. G. CAIRNEY
Affiliation:
Department of Biological Sciences, University of Western Sydney (Nepean), P.O. Box 10, Kingswood, NSW 2747, Australia
Get access

Abstract

A β-1,4-endoxylanase from the ericoid mycorrhizal fungus H. ericae has been purified to electrophoretic homogeneity using isoelectric focusing, ion exchange and gel permeation chromatography. The enzyme has an isoelectric point of 4·85–5·20 and a molecular weight of 58·4 kDa. The apparent S0·5 of the enzyme for soluble birchwood glucuronoxylan is 3·75 mg ml−1 and the Vmax 468·0 nkatal mg−1 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.

Keywords

Hymenoscyphus ericaexylanaseericoid mycorrhizal symbiosis
Type
Research Article
Information
The New Phytologist , Volume 135 , Issue 2 , February 1997 , pp. 345 - 352
Copyright
Trustees of the New Phytologist 1997

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)