Document Detail


Noncellulolytic fungal beta-glucanases: their physiology and regulation.
MedLine Citation:
PMID:  7763458     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
S M Pitson; R J Seviour; B M McDougall
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Enzyme and microbial technology     Volume:  15     ISSN:  0141-0229     ISO Abbreviation:  Enzyme Microb. Technol.     Publication Date:  1993 Mar 
Date Detail:
Created Date:  1993-04-22     Completed Date:  1993-04-22     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8003761     Medline TA:  Enzyme Microb Technol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  178-92     Citation Subset:  B    
Affiliation:
Biotechnology Research Centre, La Trobe University College of Northern Victoria, Bendigo, Australia.
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MeSH Terms
Descriptor/Qualifier:
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:
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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