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Computer-aided discovery of a novel thermophilic laccase for low-density polyethylene degradation

文献类型： 外文期刊

作者： Zhang, Yan 1 ; Plesner, Thea Jess 1 ; Ouyang, Yi 1 ; Zheng, Yu-Cong 2 ; Bouhier, Etienne 3 ; Berentzen, Emilie Ingemann 1 ; Zhang, Mingliang 1 ; Zhou, Pengfei 1 ; Zimmermann, Wolfgang 6 ; Andersen, Gregers Rom 7 ; Eser, Bekir Engin 1 ; Guo, Zheng 1 ;

作者机构： 1.Aarhus Univ, Dept Biol & Chem Engn, DK-8000 Aarhus, Denmark

2.Max Planck Inst Terr Microbiol, Karl von Fr Str 10, D-35043 Marburg, Germany

3.Univ Technol Compiegne, Dept Biol Engn, Compiegne, France

4.Fujian Normal Univ, Engn Res Ctr Ind Microbiol, Minist Educ, Fuzhou, Peoples R China

5.Guangdong Acad Agr Sci, Sericultural & Agrifood Res Inst, Key Lab Funct Foods, Guangdong Key Lab Agr Prod Proc,Minist Agr & Rural, Guangzhou 510610, Peoples R China

6.Univ Leipzig, Inst Analyt Chem, D-04103 Leipzig, Germany

7.Aarhus Univ, Dept Mol Biol & Genet, DK-8000 Aarhus, Denmark

关键词： Enzyme discovery; Laccase; Thermophilic enzyme; PE degradation; Dye decolorization

期刊名称：JOURNAL OF HAZARDOUS MATERIALS （ 影响因子：13.6； 五年影响因子：12.7 ）

ISSN： 0304-3894

年卷期： 2023 年 458 卷

页码：

收录情况： SCI

摘要： Polyethylene (PE) and industrial dyes are recalcitrant pollutants calling for the development of sustainable solutions for their degradation. Laccases have been explored for removal of contaminants and pollutants, including dye decolorization and plastic degradation. Here, a novel thermophilic laccase from PE-degrading Lysinibaccillus fusiformis (LfLAC3) was identified through a computer-aided and activity-based screening. Biochemical studies of LfLAC3 indicated its high robustness and catalytic promiscuity. Dye decolorization experiments showed that LfLAC3 was able to degrade all the tested dyes with decolorization percentage from 39% to 70% without the use of a mediator. LfLAC3 was also demonstrated to degrade low-density polyethylene (LDPE) films after eight weeks of incubation with either crude cell lysate or purified enzyme. The formation of a variety of functional groups was detected using Fourier transform infrared spectroscopy (FTIR) and X-ray photoelectron spectroscopy (XPS). Damage on the surfaces of PE films was observed via scanning electron microscopy (SEM). The potential catalytic mechanism of LfLAC3 was disclosed by structure and substrate-binding modes analysis. These findings demonstrated that LfLAC3 is a promiscuous enzyme that has promising potential for dye decolorization and PE degradation.

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