Abstract
Endoglucanase C encoded by the celC gene of Clostridium thermocellum has been purified to homogeneity from a recombinant Escherichia coli strain. It was found that this enzyme is highly efficient in degrading glucans with alternating β-1,4- and β-1,3-linkages but lacks activity on unmodified cellulosic substrates. The properties of endoglucanase C were compared to those of Bacillus subtilis β-glucanase, an enzyme used in the brewing industry for β-glucan degradation. Both enzyme cause a rapid decrease of the viscosity of barley β-glucan as a result of internal chain cleavage. Endoglucanase C hydrolyses non-specifically β-1,3- and β-1,4-bonds adjacent to unsubstituted or 4-O′-substituted cellobiose units. Due to its lower pH optimum and increased thermostability endoglucanase C compares favourably with B. subtilis β-glucanase and seems suitable for use in the mashing process of beer brewing.
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