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ORIGINAL RESEARCH article

Front. Microbiol.
Sec. Microbiotechnology
Volume 15 - 2024 | doi: 10.3389/fmicb.2024.1478305
This article is part of the Research Topic Microbial Biotechnologies for Efficient Wastewater Treatment and Resource Recovery View all 9 articles

Catalase-peroxidase StKatG2 from Salinicola tamaricis: a versatile Mn(II) oxidase that decolorizes malachite green

Provisionally accepted
Mengyao Ding Mengyao Ding Wenjing Wang Wenjing Wang Zhenkun Lu Zhenkun Lu Yuhui Sun Yuhui Sun Xinzhen Qiao Xinzhen Qiao Meixue Dai Meixue Dai Guoyan Zhao Guoyan Zhao *
  • Shandong Normal University, Jinan, China

The final, formatted version of the article will be published soon.

    Manganese (Mn) oxidation processes have garnered significant attention recently due to their potential for degrading organic pollutants. These processes are primarily catalyzed by Mn(II) oxidases. Salinicola tamaricis F01, an endophytic bacterium derived from wetland plants, has demonstrated Mn(II)-oxidizing capacity. In this study, a catalase-peroxidase, StKatG2, was cloned and overexpressed in Escherichia coli from the strain F01. The purified recombinant StKatG2 exhibited Mn(II)-oxidizing activity with Km and Kcat values of 2.529 mmol/L and 2.82 min -1 respectively. Optimal catalytic conditions for StKatG2 were observed at pH 7.5 and 55°C, with 45.1% activity retention after an 8-hour exposure to 80°C. The biogenic manganese oxides produced by StKatG2 exhibited mixed-valence states with Mn(II), including Mn(III), Mn(IV), and Mn(VII). Furthermore, StKatG2 demonstrated superior decolorization efficiency for malachite green (MG), achieving decolorization rates of 73.38% for 20 mg/L MG and 60.08% for 50 mg/L MG, while degrading MG into 4-(dimethylamino)benzophenone. Therefore, the catalase-peroxidase StKatG2 exhibits multifunctionality in Mn(II)-oxidizing activity and has the potential to serve as an environmentally friendly enzyme for MG removal.

    Keywords: Catalase-peroxidase, Mn(II) oxidases, Malachite green, Decolorization ability, Enzymic activity

    Received: 09 Aug 2024; Accepted: 21 Oct 2024.

    Copyright: © 2024 Ding, Wang, Lu, Sun, Qiao, Dai and Zhao. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Guoyan Zhao, Shandong Normal University, Jinan, China

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