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

被引:14
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 ,4 ]
Zhou, Pengfei [1 ,5 ]
Zimmermann, Wolfgang [6 ]
Andersen, Gregers Rom [7 ]
Eser, Bekir Engin [1 ]
Guo, Zheng [1 ]
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; TRAMETES-VERSICOLOR LACCASE; DYE; OXIDATION; MECHANISMS; REACTIVITY; PLASTICS; SYSTEMS; WASTE; WATER;
D O I
10.1016/j.jhazmat.2023.131986
中图分类号
X [环境科学、安全科学];
学科分类号
08 ; 0830 ;
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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页数:12
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共 73 条
[1]   Fungal laccase discovered but yet undiscovered [J].
Agrawal, Komal ;
Chaturvedi, Venkatesh ;
Verma, Pradeep .
BIORESOURCES AND BIOPROCESSING, 2018, 5
[2]   Adsorption of methylene blue dye from aqueous solution using low-cost adsorbent: kinetic, isotherm adsorption, and thermodynamic studies [J].
Al-Asadi, Safaa Talib ;
Al-Qaim, Fouad Fadhil ;
Al-Saedi, Haider Falih Shamikh ;
Deyab, Issa Farhan ;
Kamyab, Hesam ;
Chelliapan, Shreeshivadasan .
ENVIRONMENTAL MONITORING AND ASSESSMENT, 2023, 195 (06)
[3]   Laccases: structure, function, and potential application in water bioremediation [J].
Arregui, Leticia ;
Ayala, Marcela ;
Gomez-Gil, Ximena ;
Gutierrez-Soto, Guadalupe ;
Eduardo Hernandez-Luna, Carlos ;
Herrera de los Santos, Mayra ;
Levin, Laura ;
Rojo-Dominguez, Arturo ;
Romero-Martinez, Daniel ;
Saparrat, Mario C. N. ;
Trujillo-Roldan, Mauricio A. ;
Valdez-Cruz, Norma A. .
MICROBIAL CELL FACTORIES, 2019, 18 (01)
[4]  
Baffour-Awuah E., 2020, ADV COMPOS BERLIN GE, V11, P169, DOI [10.1515/9783110655049-010, DOI 10.1515/9783110655049-010]
[5]   Promoting laccase activity towards non-phenolic substrates: a mechanistic investigation with some laccase-mediator systems [J].
Baiocco, P ;
Barreca, AM ;
Fabbrini, M ;
Galli, C ;
Gentili, P .
ORGANIC & BIOMOLECULAR CHEMISTRY, 2003, 1 (01) :191-197
[6]   Sargassum myriocystum-mediated TiO2-nanoparticles and their antimicrobial, larvicidal activities and enhanced photocatalytic degradation of various dyes [J].
Balaraman, Perumal ;
Balasubramanian, Balamuralikrishnan ;
Liu, Wen-Chao ;
Kaliannan, Durairaj ;
Durai, Mahendran ;
Kamyab, Hesam ;
Alwetaishi, Mamdooh ;
Maluventhen, Viji ;
Ashokkumar, Veeramuthu ;
Chelliapan, Shreeshivadasan ;
Maruthupandian, Arumugam .
ENVIRONMENTAL RESEARCH, 2022, 204
[7]   A mini-review: current advances in polyethylene biodegradation [J].
Bardaji, Danae Kala Rodriguez ;
Moretto, Jessica Aparecida Silva ;
Furlan, Joao Pedro Rueda ;
Stehling, Eliana Guedes .
WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY, 2020, 36 (02)
[8]   Bioremediation potential of laccase for catalysis of glyphosate, isoproturon, lignin, and parathion: Molecular docking, dynamics, and simulation [J].
Bhatt, Pankaj ;
Bhatt, Kalpana ;
Chen, Wen-Juan ;
Huang, Yaohua ;
Xiao, Ying ;
Wu, Siyi ;
Lei, Qiqi ;
Zhong, Jianfeng ;
Zhu, Xixian ;
Chen, Shaohua .
JOURNAL OF HAZARDOUS MATERIALS, 2023, 443
[9]   Binding interaction of glyphosate with glyphosate oxidoreductase and C-P lyase: Molecular docking and molecular dynamics simulation studies [J].
Bhatt, Pankaj ;
Joshi, Tushar ;
Bhatt, Kalpana ;
Zhang, Wenping ;
Huang, Yaohua ;
Chen, Shaohua .
JOURNAL OF HAZARDOUS MATERIALS, 2021, 409 (409)
[10]   Construction of a biomimetic core-shell PDA@Lac bioreactor from intracellular laccase as a nano-confined biocatalyst for decolorization [J].
Bo, Hongqing ;
Zhang, Ziyan ;
Chen, Zhonglin ;
Qiao, Wenrui ;
Jing, Siyi ;
Dou, Tongtong ;
Tian, Tian ;
Zhang, Ming ;
Qiao, Weichuan .
CHEMOSPHERE, 2023, 330