The first bacterial β-1,6-endoglucanase from Saccharophagus degradans 2-40T for the hydrolysis of pustulan and laminarin
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- 作者：Damao Wang ; Do Hyoung Kim ; Eun Ju Yun…
- 关键词：β ; 1 ; 6 ; endoglucanase ; GH30 ; Hydrolysis ; Saccharophagus degradans 2 ; 40T
- 刊名：Applied Microbiology and Biotechnology
- 出版年：2017
- 出版时间：January 2017
- 年：2017
- 卷：101
- 期：1
- 页码：197-204
- 全文大小：
- 刊物类别：Chemistry and Materials Science
- 刊物主题：Microbiology; Microbial Genetics and Genomics; Biotechnology;
- 出版者：Springer Berlin Heidelberg
- ISSN：1432-0614
- 卷排序：101
文摘
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, Vmax, KM, and kcat 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.