A dye-decolorizing peroxidase from Bacillus subtilis exhibiting substrate-dependent optimum temperature for dyes and b-ether lignin dimer
- A dye-decolorizing peroxidase from Bacillus subtilis exhibiting substrate-dependent optimum temperature for dyes and b-ether lignin dimer
- 민경선; 공경택; 우한민; 김연제; 엄영순
- Issue Date
- Scientific Reports
- VOL 5, NO 8245, 1-8
- In the biorefinery using lignocellulosic biomass as feedstock, pretreatment to breakdown or loosen lignin is important step and various approaches have been conducted. For biological pretreatment, we screened Bacillus subtilis KCTC2023 as a potential lignin-degrading bacterium based on veratryl alcohol (VA) oxidation test and the putative heme-containing dye-decolorizing peroxidase was found in the genome of B. subtilis KCTC2023. The peroxidase from B. subtilis KCTC2023 (BsDyP) was capable of oxidizing various substrates and atypically exhibits substrate-dependent optimum temperature: 306C for dyes (Reactive Blue19 and Reactive Black5) and 506C for high redox potential substrates (2,29-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid [ABTS], VA, and veratryl glycerol-b-guaiacyl ether [VGE]) over 11.0 V vs. normal hydrogen electrode. At 506C, optimum temperature for high redox potential substrates, BsDyP not only showed the highest VA oxidation activity (0.13 Umg21) among the previously reported bacterial peroxidases but also successfully achieved VGE decomposition by cleaving Ca-Cb bond in the absence of any oxidative mediator with a specific activity of 0.086 Umg21 and a conversion rate of 53.5%. Based on our results, BsDyP was identified as the first bacterial peroxidase capable of oxidizing high redox potential lignin-related model compounds, especially VGE, revealing a previously unknown versatility of lignin degrading biocatalyst in nature.
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