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

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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 2-40T, 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 pH 7.0 and 40 °C, respectively. The kinetic constants of Gly30B, V max, K M, and k cat were determined to be 153.8 U/mg protein, 24.2 g/L, and 135.6 s−1 for pustulan and 32.8 U/mg protein, 100.8 g/L, and 28.9 s−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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Acknowledgements

This work was financially supported by the Advanced Biomass R&D Center of Korea (2011-0031359), funded by the Korean Government (MSIP). Experiments were carried out using the facilities of the Institute of Biomedical Science and Food Safety at the Food Safety Hall, Korea University.

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Correspondence to Kyoung Heon Kim.

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Wang, D., Kim, D.H., Yun, E.J. et al. The first bacterial β-1,6-endoglucanase from Saccharophagus degradans 2-40T for the hydrolysis of pustulan and laminarin. Appl Microbiol Biotechnol 101, 197–204 (2017). https://doi.org/10.1007/s00253-016-7753-8

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