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

Content Provider	Springer Nature Link
Author	Wang, Damao Kim, Do Hyoung Yun, Eun Ju Park, Yong Cheol Seo, Jin Ho Kim, Kyoung Heon
Copyright Year	2016
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.
Starting Page	197
Ending Page	204
Page Count	8
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	101
Issue Number	1
e-ISSN	14320614
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2016-08-12
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	β-1,6-endoglucanase GH30 Hydrolysis Saccharophagus degradans 2-40T Microbiology Microbial Genetics and Genomics Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

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