Cooperative action from Cu-centered MOF and a laccase for enhanced decolorization of synthetic dyes
文献类型： 外文期刊
作者： Plesner, Thea Jess 1 ; Wang, Fang 1 ; Yi, Ouyang 1 ; Khazaee, Zeynab 1 ; Zhou, Pengfei 1 ; Zhang, Mingliang 1 ; Eser, Bekir Engin 1 ; Zhang, Yan 1 ; Guo, Zheng 1 ;
作者机构： 1.Aarhus Univ, Dept Biol & Chem Engn, DK-8000 Aarhus, Denmark
2.Jilin Univ, Sch Life Sci, Key Lab Mol Enzymol & Engn, Minist Educ, Changchun 130021, Peoples R China
3.Guangdong Acad Agr Sci, Sericultural & Agri Food Res Inst, Guangdong Key Lab Agr Prod Proc, Key Lab Funct Foods,Minist Agr & Rural Affairs, Guangzhou 510610, Peoples R China
4.Fujian Normal Univ, Engn Res Ctr Ind Microbiol, Minist Educ, Fuzhou, Peoples R China
关键词： Laccase; Lysinibacillus fusiformis; Metal-organic framework (MOF); Copper center; Decolorization; Detoxification
期刊名称：BIOCHEMICAL ENGINEERING JOURNAL （ 影响因子：3.8； 五年影响因子：3.7 ）
ISSN： 1369-703X
年卷期： 2025 年 221 卷
页码：
收录情况： SCI
摘要： Laccases are highly versatile copper-dependent enzymes that can oxidize a broad range of substrates, with the combination of converting molecular oxygen to water. However, extreme conditions cause laccase instability, inactivation, and difficulty in its applications. Applying nanomaterials to natural laccase immobilization is essential for their applications as it allows their stabilization and easy recovery from the liquid reaction media and subsequent reuse. Here, we develop an ingenious method to cooperate the copper centers of a copper-based metal-organic framework (Cu-MOF) and a newly discovered laccase-LfLAC3 for effective decolorization of synthetic dyes. The immobilized enzyme presents excellent properties: the catalytic activity improved 62.6-fold, and the half-life (t1/2) at 60 degrees C increased more than 3-fold, indicating enhanced stability. The reusability was tested by monitoring the decolorization efficiency towards malachite green at 30 degrees C and 60 degrees C, which demonstrated that the immobilized LfLAC3 can be reused more than ten cycles with more than 80 % removal at both temperatures through a simple centrifugation process. In addition, the detoxification of dyes after enzymatic treatment was also investigated by toxicity assessment. The structural characterization results indicated that copper centers of Cu-MOFs were evenly distributed in MOF-enzyme composites, affording synergistic effects for the catalytic functions. Our work highlights the potential of cooperating metal centers of MOFs and metal enzymes to generate catalysts with promising catalytic properties.
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