Abstract
Chitosanases play an important role in chitosan degradation, and the enzymatic degradation products of chitosan show various biological activities. Here, a novel glycoside hydrolase family 46 chitosanase (named Csn-BAC) from Bacillus sp. MD-5 was heterologously expressed in Escherichia coli BL21 (DE3). The recombinant enzyme was purified by Ni-NTA affinity chromatography, and its molecular weight was estimated to be 35 kDa by SDS-PAGE. Csn-BAC showed maximal activity toward colloidal chitosan at pH 7 and 40 °C. The enzymatic activity of Csn-BAC was enhanced by Mn2+, Cu2+ and Co2+ at 1 mM, and by Mn2+ at 5 mM. Thin-layer chromatography and electrospray ionization-mass spectrometry results demonstrated that Csn-BAC exhibited an endo-type cleavage pattern and hydrolyzed chitosan to yield, mainly, (GlcN)2 and (GlcN)3. The enzymatic properties of this chitosanase may make it a good candidate for use in oligosaccharide production-based industries.
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