Purification and characterization of a β-1,4-endoxylanase from the ericoid mycorrhizal fungus Hymenoscyphus ericae.
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| Title: | Purification and characterization of a β-1,4-endoxylanase from the ericoid mycorrhizal fungus Hymenoscyphus ericae. |
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| Authors: | Burke, R. M.1 Ron.Burke@umist.ac.uk, Cairney, J. W. G.2 |
| Source: | New Phytologist. Feb97, Vol. 135 Issue 2, p345-352. 8p. |
| Subjects: | Xylanases, Mycorrhizal fungi, Isoelectric focusing, Electrophoresis, Ion exchange (Chemistry), Gel permeation chromatography |
| 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 4.85-5.2O 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. [ABSTRACT FROM AUTHOR] |
| Copyright of New Phytologist is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 12500019 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Purification and characterization of a β-1,4-endoxylanase from the ericoid mycorrhizal fungus <em>Hymenoscyphus ericae</em>. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Burke%2C+R%2E+M%2E%22">Burke, R. M.</searchLink><relatesTo>1</relatesTo><i> Ron.Burke@umist.ac.uk</i><br /><searchLink fieldCode="AR" term="%22Cairney%2C+J%2E+W%2E+G%2E%22">Cairney, J. W. G.</searchLink><relatesTo>2</relatesTo> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22New+Phytologist%22">New Phytologist</searchLink>. Feb97, Vol. 135 Issue 2, p345-352. 8p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Xylanases%22">Xylanases</searchLink><br /><searchLink fieldCode="DE" term="%22Mycorrhizal+fungi%22">Mycorrhizal fungi</searchLink><br /><searchLink fieldCode="DE" term="%22Isoelectric+focusing%22">Isoelectric focusing</searchLink><br /><searchLink fieldCode="DE" term="%22Electrophoresis%22">Electrophoresis</searchLink><br /><searchLink fieldCode="DE" term="%22Ion+exchange+%28Chemistry%29%22">Ion exchange (Chemistry)</searchLink><br /><searchLink fieldCode="DE" term="%22Gel+permeation+chromatography%22">Gel permeation chromatography</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: 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 S0.5 of the enzyme for soluble birchwood glucuronoxylan is 3.75 mg ml-1 and the <em>V</em>max 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. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of New Phytologist is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1046/j.1469-8137.1997.00634.x Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 8 StartPage: 345 Subjects: – SubjectFull: Xylanases Type: general – SubjectFull: Mycorrhizal fungi Type: general – SubjectFull: Isoelectric focusing Type: general – SubjectFull: Electrophoresis Type: general – SubjectFull: Ion exchange (Chemistry) Type: general – SubjectFull: Gel permeation chromatography Type: general Titles: – TitleFull: Purification and characterization of a β-1,4-endoxylanase from the ericoid mycorrhizal fungus <em>Hymenoscyphus ericae</em>. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Burke, R. M. – PersonEntity: Name: NameFull: Cairney, J. W. G. IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 02 Text: Feb97 Type: published Y: 1997 Identifiers: – Type: issn-print Value: 0028646X Numbering: – Type: volume Value: 135 – Type: issue Value: 2 Titles: – TitleFull: New Phytologist Type: main |
| ResultId | 1 |
