Min, Kyoungseon Gong, Gyeongtaek Woo, Han Min Kim, Yunje Um, Youngsoon 2024-01-20T08:00:14Z 2024-01-20T08:00:14Z 2021-09-05 2015-02 2045-2322 https://pubs.kist.re.kr/handle/201004/125808 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: 30 degrees C for dyes (Reactive Blue19 and Reactive Black5) and 50 degrees C for high redox potential substrates (2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid [ABTS], VA, and veratryl glycerol-beta-guaiacyl ether [VGE]) over +1.0 V vs. normal hydrogen electrode. At 50 degrees C, optimum temperature for high redox potential substrates, BsDyP not only showed the highest VA oxidation activity (0.13 Umg(-1)) among the previously reported bacterial peroxidases but also successfully achieved VGE decomposition by cleaving C-alpha-C-beta bond in the absence of any oxidative mediator with a specific activity of 0.086 Umg(-1) 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. English Nature Publishing Group A dye-decolorizing peroxidase from Bacillus subtilis exhibiting substrate-dependent optimum temperature for dyes and beta-ether lignin dimer Article 10.1038/srep08245 1 Scientific Reports, v.5 Scientific Reports 5 Y scie scopus 000348768100017 2-s2.0-84942888204 Multidisciplinary Sciences Science & Technology - Other Topics Article PHANEROCHAETE-CHRYSOSPORIUM VERSATILE-PEROXIDASE MANGANESE PEROXIDASE PLEUROTUS-ERYNGII OXIDATION SITES IRPEX-LACTEUS ACID IDENTIFICATION PURIFICATION BIODEGRADATION