Cited by 127Fungal and yeast genetics researchEnzyme Production and CharacterizationBiofuel production and bioconversion

Biochemistry and molecular biology of exocellular fungal β-(1,3)- and β-(1,6)-glucanases

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Martin, Kirstee, McDougall, Barbara M., McIlroy, Simon, Jayus, Chen, Jiezhong, Seviour, Robert J.·2007·FEMS Microbiology Reviews

Abstract

Many fungi produce exocellular beta-glucan-degrading enzymes, the beta-glucanases including the noncellulolytic beta-(1,3)- and beta-(1,6)-glucanases, degrading beta-(1,3)- and beta-(1,6)-glucans. An ability to purify several exocellular beta-glucanases attacking the same linkage type from a single fungus is common, although unlike the beta-1,3-glucanases, production of multiple beta-1,6-glucanases is quite rare in fungi. Reasons for this multiplicity remain unclear and the multiple forms may not be genetically different but arise by posttranslational glycosylation or proteolytic degradation of the single enzyme. How their synthesis is regulated, and whether each form is regulated differentially also needs clarifying. Their industrial potential will only be realized when the genes encoding them are cloned and expressed in large quantities. This review considers what is known in molecular terms about their multiplicity of occurrence, regulation of synthesis and phylogenetic diversity. It discusses how this information assists in understanding their functions in the fungi producing them. It deals largely with exocellular beta-glucanases which here refers to those recoverable after the cells are removed, since those associated with fungal cell walls have been reviewed recently by Adams (2004). It also updates the earlier review by Pitson et al. (1993).

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Crossref · 10.1111/j.1574-6976.2006.00055.x

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  • Hydrolysis of laminarin and chrysolaminarin is catalyzed by four enzymes: endo-β-(1→6) glucanases, endo-β-(1→3) glucanases, exo-β-(1→3) glucanases, and β-glucosidases.

    “Hydrolysis of laminarin and chrysolaminarin is catalyzed by the action of four enzymes: endo-β-(1→6) glucanases (EC 3.2.1.75),endo-β-(1→3) glucanases (EC 3.2.1.39),exo-β-(1→3) glucanases (EC 3.2.1.58),and β-glucosidases (EC 3.2.1.21).”

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2 of the 147 references couldn’t be matched to a known paper.

Research works printed but not linked: 3

  1. I.U.B (1992) Enzyme Nomenclature; Recommendations of the Nomenclature Committee of the International Union of Biochemistry. Academic Press, Orlando.
  2. Reese E & Mandels M (1963) Enzymic hydrolysis of b-glucans. Advances in Enzymic Hydrolysis of Cellulose and Related Materials (Reese E, ed), pp. 197-234. Pergamon Press, Oxford.
  3. van Rensburg P & Pretorius IS (2000) Enzymes in wine making: harnessing natural catalysts for efficient biotransformations - a review. S Afr J Enol Vitic 21: 52-73.

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Authors
Martin, K., McDougall, B. M., McIlroy, S., Jayus, Chen, J., & Seviour, R. J.
Affiliations
  • University of Dundee (GB)
  • La Trobe University (AU)
Venue
FEMS Microbiology Reviews
Published
2007-03
Volume
31
Issue
2
Pages
168-192
ISSN
  • 0168-6445 (ISSN-L)
  • 1574-6976
OpenAlex
W1972589860
Cited by
127
References
147
Citations by year
2026: 2 · 2025: 4 · 2024: 7 · 2023: 8 · 2022: 11 · 2021: 11 · 2020: 9 · 2019: 7 · 2018: 6 · 2017: 6 · 2016: 7 · 2015: 5 · 2014: 6 · 2013: 8 · 2012: 3
FWCI
2.78
Type
journal article
Language
en
Open access
Locations
  • FEMS Microbiology Reviews (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Physical Sciences › Engineering › Biomedical Engineering › Biofuel production and bioconversion
Keywords
β-glucanase, β-1,3-glucanase, β-1,6-glucanase, extracellular enzymes, fungal enzymes, post-translational glycosylation, proteolysis, enzyme regulation, gene cloning, industrial enzymes, phylogenetic diversity, fungal cell wall
MeSH terms
Amino Acid Sequence, Binding Sites, Carbon, Cell Wall, Fermentation, Fungi, Glycoside Hydrolases, Introns, Molecular Sequence Data, Nitrogen, Phylogeny, Conserved Sequence, Amino Acid Motifs, Protein Sorting Signals, Glucan 1,3-beta-Glucosidase, beta-Glucans

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