Biochemical properties and application of a novel β-1,3-1,4-glucanase from Paenibacillus barengoltzii

  • Food Chem. 2017 Nov 1:234:68-75. doi: 10.1016/j.foodchem.2017.04.162.
Bin Zhang  1 ,  Yu Liu  2 ,  Hongye Yang  2 ,  Qiaojuan Yan  3 ,  Shaoqing Yang  2 ,  Zheng-Qiang Jiang  4 ,  Shaozhen Li  5
Affiliations
  • 1. College of Food and Bioengineering, Henan University of Science and Technology, Luoyang 471023, China; Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
  • 2. Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
  • 3. College of Engineering, China Agricultural University, Beijing 100083, China.
  • 4. Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China. Electronic address: [email protected].
  • 5. Beijing Huiyuan Food & Beverage Co., Ltd., Beijing 101305, China.
PMID: 28551269 DOI: 10.1016/j.foodchem.2017.04.162
Abstract

A novel endo-β-1,3-1,4-glucanase gene (PbBglu16A) was cloned from Paenibacillus barengoltzii and heterogeneously expressed in Escherichia coli. The recombinant β-1,3-1,4-glucanase (PbBglu16A) was purified to homogeneity with a recovery yield of 78.6% and a specific activity of 431.8Umg-1. The molecular mass of PbBglu16A was estimated to be 44.0kDa by SDS-PAGE. The optimal pH and temperature of PbBglu16A were 6.0 and 55°C, respectively. The enzyme was stable within pH 3.5-9.0 and up to 55°C. PbBglu16A exhibited high substrate specificity towards barley β-glucan, OAT β-glucan and lichenin. PbBglu16A showed an endo-type cleavage pattern and hydrolyzed endogenous enzyme-deactivated OAT bran into β-gluco-oligosaccharides with a yield of 7.0%, which mainly consisted of trioligosaccharide and tetraoligosaccharide. Further, PbBglu16A could promote mashing with a reduced filtration time (14.0%) and viscosity (3.4%). Thus, PbBglu16A might be a promising candidate for the production of β-gluco-oligosaccharides and in brewing industry.

Keywords
Brewing; Characterization; Gene cloning; Paenibacillus barengoltzii; β-1,3-1,4-Glucanase; β-Gluco-oligosaccharides.
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