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

• Published in: Molecules (Basel, Switzerland) Vol. 27; no. 24; p. 8660
• Main Authors: Wu, Guang-Rong, Sun, Li-Juan, Xu, Jia-Kun, Gao, Shu-Qin, Tan, Xiang-Shi, Lin, Ying-Wu
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01.12.2022; MDPI
• Subjects: Anti-Bacterial Agents - pharmacology; Antibiotics; Antiinfectives and antibacterials; Biodegradation; Catalysis; China; Chlortetracycline; degradation; Degradation products; Doxycycline; Environmental cleanup; Environmental degradation; Environmental engineering; environmental remediation; Enzymes; Escherichia coli - genetics; Escherichia coli - metabolism; Health risks; Heme; Heme - chemistry; heme enzyme; Humans; Hydrogen Peroxide; Liquid chromatography; Manganese; Microorganisms; Myoglobin; Myoglobin - chemistry; Myoglobins; Nonprescription drugs; Oxidants; Oxidation; Oxidizing agents; Oxytetracycline; Peroxidase; Peroxidases - chemistry; Pollutants; Tetracycline; Tetracyclines; Toxicity; Wastewater; Water pollution; China; environmental remediation; degradation; antibiotics; myoglobin; heme enzyme
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules27248660

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 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 ~100%, ~98%, ~94%, and ~90%, respectively, within 5 min by using H O 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 . Therefore, this study indicates that the engineered heme enzyme has potential applications for environmental remediation by degradation of tetracycline antibiotics.