Heterologous expression and characterization of thermostable chitinase and beta-N-acetylhexosaminidase from Caldicellulosiruptor acetigenus and their synergistic action on the bioconversion of chitin into N-acetyl-D-glucosamine

文献类型： 外文期刊

第一作者： Qin, Xing

作者： Qin, Xing;Xin, YanZhe;Su, Xiaoyun;Wang, Xiaolu;Zhang, Jie;Tu, Tao;Wang, Yaru;Yao, Bin;Huang, Huoqing;Luo, Huiying

作者机构：

关键词： Chitinase; beta-N-acetylhexosaminidase; N-acetyl-D-glucosamine

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：6.953； 五年影响因子：6.737 ）

ISSN： 0141-8130

年卷期： 2021 年 192 卷

页码：

收录情况： SCI

摘要： The bioconversion of chitin into N-acetyl-D-glucosamine (GlcNAc) using chitinolytic enzymes is one of the important avenues for chitin valorization. However, industrial applications of chitinolytic enzymes have been limited by their poor thermostability. Therefore, it is necessary to discover thermostable chitinolytic enzymes for GlcNAc production from chitin. In this study, two chitinolytic enzyme-encoding genes CaChiT and CaHex from Caldicellulosiruptor acetigenus were identified and heterologously expressed in Escherichia coli. The purified re-combinant CaChiT and CaHex showed optimal activities at 70 degrees C and 90 degrees C respectively, and exhibited good thermostability over a range of temperature below 70 degrees C and broad pH stability at pH range of 3.0-8.0. CaChiT and CaHex were active on colloidal chitin, pNP-(GlcNAc)(2), pNP-(GlcNAc)(3), and pNP-GlcNAc, pNP-(GlcNAc)2, pNP-(GlcNAc)(3), pNP-Glc respectively. Besides, the chitin oligosaccharides and colloidal chitin hydrolysis profiles revealed that CaChiT degraded chitin chains through exo-mode of action. Furthermore, CaChiT and CaHex exhibited a synergistic effect in the degradation of colloidal chitin, reaching 0.60 mg/mL of GlcNAc production after 1 h incubation. These results suggested that a combination of CaChiT and CaHex have great potential for industrial applications in the enzymatic production of GlcNAc from chitin-containing biowastes.

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