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Updated: Sep 15, 2026

High Throughput Screening of Fungal Endoglucanase Activity in Escherichia coli
Published on: August 13, 2011
Studies on beta-glucanases. Some properties of a bacterial endo-beta-(1 leads to 3)-glucanase system
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 beta-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 beta-glucanases, an endo-beta-(1-->3)-glucanase and an endo-beta-(1-->4)-glucanase. The two enzymes occur in both high- and low-molecular-weight forms, the latter endo-beta-(1-->3)-glucanase having a molecular weight of about 16000.

