Characterization of a Highly Thermostable and Organic Solvent-Tolerant Copper-Containing Polyphenol Oxidase with Dye-Decolorizing Ability from Kurthia huakuii LAM0618(T)

文献类型： 外文期刊

第一作者： Guo, Xiang

作者： Guo, Xiang;Zhou, Shan;Wang, Huimin;Kong, Delong;Zhu, Jie;Dong, Weiwei;Ruan, Zhiyong;Guo, Xiang;Wang, Yanwei;He, Mingxiong;Hu, Guoquan;Song, Jinlong

作者机构：

期刊名称：PLOS ONE （ 影响因子：3.24； 五年影响因子：3.788 ）

ISSN： 1932-6203

年卷期： 2016 年 11 卷 10 期

页码：

收录情况： SCI

摘要： Laccases are green biocatalysts that possess attractive advantages for the treatment of resistant environmental pollutants and dye effluents. A putative laccase-like gene, laclK, encoding a protein of 29.3 kDa and belonging to the Cu-oxidase_4 superfamily, was cloned and overexpressed in Escherichia coli. The purified recombinant protein LaclK (LaclK) was able to oxidize typical laccase substrates such as 2,6-dimethoxyphenol and L-dopamine. The characteristic adsorption maximums of typical laccases at 330 nm and 610 nm were not detected for LaclK. Cu2+ was essential for substrate oxidation, but the ratio of copper atoms/molecule of LaclK was determined to only be 1: 1. Notably, the optimal temperature of LaclK was 85 degrees C with 2,6-dimethoxyphenol as substrates, and the half-life approximately 3 days at 80 degrees C. Furthermore, 10% (v/v) organic solvents (methanol, ethanol, isopropyl alcohol, butyl alcohol, Triton x-100 or dimethyl sulfoxide) could promote enzymatic activity. LaclK exhibited wide-spectrum decolorization ability towards triphenylmethane dyes, azo dyes and aromatic dyes, decolorizing 92% and 94% of Victoria Blue B (25 mu M) and Ethyl Violet (25 mu M), respectively, at a concentration of 60 U/L after 1 h of incubation at 60 degrees C. Overall, we characterized a novel thermostable and organic solvent-tolerant copper-containing polyphenol oxidase possessing dye-decolorizing ability. These unusual properties make LaclK an alternative for industrial applications, particularly processes that require high-temperature conditions.

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