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. 1973 Sep;135(1):11–18. doi: 10.1042/bj1350011

Studies on β-glucanases. Some properties of a bacterial endo-β-(1→3)-glucanase system

David J Manners 1, Glynn Wilson 1
PMCID: PMC1165783  PMID: 4776863

Abstract

A commercial enzyme preparation, originally obtained from a Flavobacterium(Cytophaga), was fractionated by continuous electrophoresis, giving a protein fraction which hydrolysed laminarin, carboxymethylpachyman, barley β-glucan, lichenin and cellodextrin in random fashion. This enzymic activity was not very stable. Ion-exchange chromatography and molecular-sieve chromatography on Bio-Gel P-60 showed that this activity was due to two specific β-glucanases, an endo-β-(1→3)-glucanase and an endo-β-(1→4)-glucanase. The two enzymes occur in both high- and low-molecular-weight forms, the latter endo-β-(1→3)-glucanase having a molecular weight of about 16000.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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