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

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

doi:10.1016/j.jhazmat.2023.131986

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

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Zheng, Yu-Cong
Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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https://doi.org/10.1016/j.jhazmat.2023.131986
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Citation

Zhang, Y., Plesner, T. J., Ouyang, Y., Zheng, Y.-C., Bouhier, E., Berentzen, E. I., et al. (2023). Computer-aided discovery of a novel thermophilic laccase for low-density polyethylene degradation. Journal of Hazardous Materials, 458: 131986. doi:10.1016/j.jhazmat.2023.131986.

Cite as: https://hdl.handle.net/21.11116/0000-000D-80ED-7

Abstract

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.