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

Damao Wang, Do Hyoung Kim, Eun Ju Yun, Yong Cheol Park, Jin Ho Seo, Kyoung Heon Kim

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

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, 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.

Original languageEnglish
Pages (from-to)1-8
Number of pages8
JournalApplied Microbiology and Biotechnology
DOIs
Publication statusAccepted/In press - 2016 Aug 12

Keywords

  • GH30
  • Hydrolysis
  • Saccharophagus degradans 2-40
  • β-1,6-endoglucanase

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

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