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.
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