| Noncellulolytic fungal beta-glucanases: their physiology and regulation. | |
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MedLine Citation:
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PMID: 7763458 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The occurrence, regulation, and action of fungal enzymes capable of degrading noncellulosic beta-glucans, especially 1,3-beta- and 1,6-beta-glucans, are reviewed. Special consideration is given to their roles in both metabolic and morphogenetic events in the fungal cell, including cell wall extension, hyphal branching, sporulation, budding, and autolysis. Also examined are the protocols currently available for their purification, with some of the properties of purified beta-glucanases discussed in terms of their potential applications in industrial, agricultural, and medical fields. |
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Authors:
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S M Pitson; R J Seviour; B M McDougall |
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Publication Detail:
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Type: Journal Article; Review |
Journal Detail:
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Title: Enzyme and microbial technology Volume: 15 ISSN: 0141-0229 ISO Abbreviation: Enzyme Microb. Technol. Publication Date: 1993 Mar |
Date Detail:
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Created Date: 1993-04-22 Completed Date: 1993-04-22 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8003761 Medline TA: Enzyme Microb Technol Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 178-92 Citation Subset: B |
Affiliation:
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Biotechnology Research Centre, La Trobe University College of Northern Victoria, Bendigo, Australia. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Biotechnology Carbohydrate Sequence Fungi / enzymology*, growth & development Glucan 1,3-beta-Glucosidase Glucans / chemistry Glycoside Hydrolases / isolation & purification, physiology* Molecular Sequence Data Substrate Specificity beta-Glucosidase / physiology |
| Chemical | |
Reg. No./Substance:
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0/Glucans; EC 3.2.1.-/Glycoside Hydrolases; EC 3.2.1.21/beta-Glucosidase; EC 3.2.1.58/Glucan 1,3-beta-Glucosidase; EC 3.2.1.75/endo-1,6-beta-glucanase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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