Efficient Degradation of Tetracycline Antibiotics by Engineered Myoglobin with High Peroxidase Activity

文献类型： 外文期刊

第一作者： Wu, Guang-Rong

作者： Wu, Guang-Rong;Lin, Ying-Wu;Sun, Li-Juan;Gao, Shu-Qin;Lin, Ying-Wu;Xu, Jia-Kun;Tan, Xiang-Shi

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关键词： heme enzyme; myoglobin; antibiotics; degradation; environmental remediation

期刊名称：MOLECULES （ 影响因子：4.927； 五年影响因子：5.11 ）

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年卷期： 2022 年 27 卷 24 期

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收录情况： SCI

摘要： Tetracyclines are one class of widely used antibiotics. Meanwhile, due to abuse and improper disposal, they are often detected in wastewater, which causes a series of environmental problems and poses a threat to human health and safety. As an efficient and environmentally friendly method, enzymatic catalysis has attracted much attention. In previous studies, we have designed an efficient peroxidase (F43Y/P88W/F138W Mb, termed YWW Mb) based on the protein scaffold of myoglobin (Mb), an O-2 carrier, by modifying the heme active center and introducing two Trp residues. In this study, we further applied it to degrade the tetracycline antibiotics. Both UV-Vis and HPLC studies showed that the triple mutant YWW Mb was able to catalyze the degradation of tetracycline, oxytetracycline, doxycycline, and chlortetracycline effectively, with a degradation rate of similar to 100%, similar to 98%, similar to 94%, and similar to 90%, respectively, within 5 min by using H2O2 as an oxidant. These activities are much higher than those of wild-type Mb and other heme enzymes such as manganese peroxidase. As further analyzed by UPLC-ESI-MS, we identified multiple degradation products and thus proposed possible degradation mechanisms. In addition, the toxicity of the products was analyzed by using in vitro antibacterial experiments of E. coli. Therefore, this study indicates that the engineered heme enzyme has potential applications for environmental remediation by degradation of tetracycline antibiotics.

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