An alkaline thermostable laccase from termite gut associated strain of Bacillus stratosphericus.
An alkaline thermostable laccase from termite gut associated strain of Bacillus stratosphericus.
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DOI:
10.1016/j.ijbiomac.2021.02.205
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发表时间:
2021-03
影响因子:
8.2
通讯作者:
Yuanxi Xiao;Jing Li;Pengju Wu;Na Ning;Jingjing Li;Yulong Shen;Qihong Huang;J. Ni
中科院分区:
文献类型:
--
作者:
Yuanxi Xiao;Jing Li;Pengju Wu;Na Ning;Jingjing Li;Yulong Shen;Qihong Huang;J. Ni
Laccase, an important oxidoreductase, is widely distributed in various organisms. Termites are known to decompose lignocellulose efficiently with the aid of gut microorganisms. However, few laccases have been characterized from termite or its gut microbes. We aimed to screen the strain capable of degrading lignocellulose from fungus-growing termites. In this study,BacillusstratosphericusBCMC2 with lignocellulolytic activity was firstly isolated from the hindgut of fungus-growing termiteMacrotermesbarneyi. The laccase gene (BaCotA) was cloned both from the BCMC2 strain and termite intestinal metagenomic DNA.BaCotAwas overexpressed inE.coli, and the recombinant BaCotA showed high specific activity (554.1 U/mg). BaCotA was thermostable with an optimum temperature of 70 °C, pH 5.0. Furthermore, BaCotA was resistant to alkali and organic solvents. The enzyme remained more than 70% residual activity at pH 8.0 for 120 min; and the organic solvents such as methanol, ethanol and acetone (10%) had no inhibitory effect on laccase activity. Additionally, BaCotA exhibited efficient decolorization ability towards indigo and crystal violet. The multiple enzymatic properties suggested the presented laccase as a potential candidate for industrial applications. Moreover, this study highlighted that termite intestine is a good resource for either new strains or enzymes.