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Applied microbiology and biotechnology

The first bacterial β-1,6-endoglucanase from Saccharophagus degradans 2-40(T) for the hydrolysis of pustulan and laminarin.


PMID 27521023

Abstract

β-1,6-glucan is a polysaccharide found in brown macroalgae and fungal cell walls. In this study, a β-1,6-endoglucanase gene from Saccharophagus degradans 2-40(T), gly30B, was cloned and overexpressed in Escherichia coli. Gly30B, which belongs to the glycoside hydrolase family 30 (GH30), was found to possess β-1,6-endoglucanase activity by hydrolyzing β-1,6-glycosidic linkages of pustulan (β-1,6-glucan derived from fungal cell walls) and laminarin (β-1,3-glucan with β-1,6-branchings, derived from brown macroalgae) to produce gentiobiose and glucose as the final products. The optimal pH and temperature for Gly30B activity were found to be pHxa07.0 and 40xa0°C, respectively. The kinetic constants of Gly30B, V max, K M, and k cat were determined to be 153.8xa0U/mg protein, 24.2xa0g/L, and 135.6xa0s(-1) for pustulan and 32.8xa0U/mg protein, 100.8xa0g/L, and 28.9xa0s(-1) for laminarin, respectively. To our knowledge, Gly30B is the first β-1,6-endoglucanase characterized from bacteria. Gly30B can be used to hydrolyze β-1,6-glucans of brown algae or fungal cell walls for producing gentiobiose as a high-value sugar and glucose as a fermentable sugar.

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