A dye-decolorizing peroxidase from Bacillus subtilis exhibiting substrate-dependent optimum temperature for dyes and b-ether lignin dimer

Title
A dye-decolorizing peroxidase from Bacillus subtilis exhibiting substrate-dependent optimum temperature for dyes and b-ether lignin dimer
Authors
민경선공경택우한민김연제엄영순
Issue Date
2015-02
Publisher
Scientific Reports
Citation
VOL 5, NO 8245, 1-8
Abstract
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.
URI
http://pubs.kist.re.kr/handle/201004/49368
ISSN
20452322
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KIST Publication > Article
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