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Construction of artificial peroxidase based on myoglobin scaffold for efficient degradation of meloxicam

文献类型： 外文期刊

作者： Zhang, Weikang 1 ; Yang, Yadan 1 ; Meng, Xiangmin 2 ; Wang, Fang 1 ; Lin, Ying-Wu 3 ; Xu, Jiakun 1 ;

作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao Marine Sci & Technol Ctr, State Key Lab Mariculture Biobreeding & Sustainabl, Qingdao 266237, Peoples R China

2.Qingdao Univ Sci & Technol, Coll Marine Sci & Biol Engn, Qingdao 266042, Peoples R China

3.Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China

关键词： Meloxicam; Myoglobin; Biodegradation; Structure-function relationship; Degradation; Environmental remediation

期刊名称：JOURNAL OF INORGANIC BIOCHEMISTRY （ 影响因子：3.2； 五年影响因子：3.6 ）

ISSN： 0162-0134

年卷期： 2025 年 262 卷

页码：

收录情况： SCI

摘要： A novel artificial peroxidase has been developed for the efficient degradation of the non-steroidal anti-inflammatory drug meloxicam by combining computer simulation and genetic engineering techniques. The results showed that the artificial peroxidase was able to completely degrade meloxicam within 90 s, with a degradation rate of 100 %, which was much higher than that of natural lacquer (46 %). The reaction time of the artificial enzyme was significantly shorter than that of natural peroxidase (10 min) and laccase (48 h). Further studies showed that the amino acid arrangement of the active site of the protein plays an important role in the catalytic performance. The degradation pathway of meloxicam was revealed using UPLC-MS analysis. In vitro toxicity assay showed complete disappearance of toxicity after meloxicam degradation. Therefore, the biocatalytic system proved to be an effective route for the green degradation of meloxicam with important application potential.

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