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Per822: A pH-stable metagenome-derived perhydrolase for dye decolorization, oil stain removal, and benzo[a]pyrene
Bing-Xue Dong1, Yi-Jia Liu2, Shao-Hui Liu1
1School of Life Science and Technology, Nanyang Normal University, Nanyang 473061, Henan, PR China.
Abstract:
Per822, a newly discovered metagenomic perhydrolase, merges promiscuous catalysis with exceptional robustness, unlocking versatile solutions for sustainable chemistry. The results revealed that Per822 possesses both esterase and peroxidase activities. Its esterase activity was optimal at pH 8.5 and 40 °C, while its peroxidase activity reached optimal levels at pH 4.5 and 45 °C. Additionally, Per822 demonstrated stability across a broad pH and temperature range. It also retained high activity in various surfactants and organic solvents, highlighting its potential for industrial applications. Application studies showed that Per822 effectively removed chili oil stains from cotton fabric when used as a laundry additive. In dye decolorization experiments, Per822 achieved efficient decolorization of multiple dyes after the addition of Br- and Fe2+. Notably, in the degradation of benzo(a)pyrene (BaP), the peracetic acid generated by Per822 (at a concentration of 64 mM) achieved a degradation rate of 99.06 % within 72 h. Subsequent plant and microbial toxicity tests indicated a significant reduction in the toxicity of the BaP degradation products. In conclusion, Per822, with its multifunctionality, stability, and outstanding performance in laundry, dye decolorization, and environmental remediation, shows great potential as a candidate enzyme for various applications in industries such as detergents, environmental repair, and organic synthesis.
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