Author:
Cui Dandan,Yang Jin,Lu Bosi,Shen Hong
Abstract
Chitosanase plays a vital role in bioactive chitooligosaccharide preparation. Here, we characterized and prepared a potential GH46 family chitosanase from Bacillus atrophaeus BSS. The purified recombinant enzyme Csn-SH showed a molecular weight of 27.0 kDa. Csn-SH displayed maximal activity toward chitosan at pH 5.0 and 45°C. Thin-layer chromatography and electrospray ionization–mass spectrometry indicated that Csn-SH mainly hydrolyzed chitosan into (GlcN)2, (GlcN)3, and (GlcN)4 with an endo-type cleavage pattern. Molecular docking analysis demonstrated that Csn-SH cleaved the glycoside bonds between subsites −2 and + 1 of (GlcN)6. Importantly, the chitosan hydrolysis rate of Csn-SH reached 80.57% within 40 min, which could reduce time and water consumption. The hydrolysates prepared with Csn-SH exhibited a good antifungal activity against Magnaporthe oryzae and Colletotrichum higginsianum. The above results suggested that Csn-SH could be used to produce active chitooligosaccharides efficiently that are biocontrol agents applicable for safe and sustainable agricultural production.
Funder
National Key Research and Development Program of China
Science and Technology Planning Project of Guangdong Province
Subject
Microbiology (medical),Microbiology
Cited by
15 articles.
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