Journal ArticleDOI
New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: towards biotechnological applications
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Spectroscopic, catalytic, and stability fingerprints of two new bacterial dye-decolorizing peroxidases (DyPs) from Bacillus subtilis and Pseudomonas putida MET94 are provided to guide future optimization of the biocatalytis towards their utilization in the fields of environmental or industrial biotechnology.Abstract:
This work provides spectroscopic, catalytic, and stability fingerprints of two new bacterial dye-decolorizing peroxidases (DyPs) from Bacillus subtilis (BsDyP) and Pseudomonas putida MET94 (PpDyP). DyPs are a family of microbial heme-containing peroxidases with wide substrate specificity, including high redox potential aromatic compounds such as synthetic dyes or phenolic and nonphenolic lignin units. The genes encoding BsDyP and PpDyP, belonging to subfamilies A and B, respectively, were cloned and heterologously expressed in Escherichia coli. The recombinant PpDyP is a 120-kDa homotetramer while BsDyP enzyme consists of a single 48-kDa monomer. The optimal pH of both enzymes is in the acidic range (pH 4–5). BsDyP has a bell-shape profile with optimum between 20 and 30 °C whereas PpDyP shows a peculiar flat and broad (10–30 °C) temperature profile. Anthraquinonic or azo dyes, phenolics, methoxylated aromatics, and also manganese and ferrous ions are substrates used by the enzymes. In general, PpDyP exhibits higher activities and accepts a wider scope of substrates than BsDyP; the spectroscopic data suggest distinct heme microenvironments in the two enzymes that might account for the distinctive catalytic behavior. However, the Bs enzyme with activity lasting for up to 53 h at 40 °C is more stable towards temperature or chemical denaturation than the PpDyP. The results of this work will guide future optimization of the biocatalytis towards their utilization in the fields of environmental or industrial biotechnology.read more
Citations
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Opportunities and challenges in biological lignin valorization
TL;DR: This perspective describes research opportunities and challenges ahead for this new field of research, which holds significant promise towards a biorefinery concept wherein polysaccharides and lignin are treated as equally valuable feedstocks.
Journal ArticleDOI
Bacterial enzymes involved in lignin degradation.
TL;DR: An overview of recent advances in the identification and use of bacterial enzymes acting on lignin or lignIn-derived products is provided, including DyP-type peroxidases and laccases.
Journal ArticleDOI
Towards lignin consolidated bioprocessing: simultaneous lignin depolymerization and product generation by bacteria†
Davinia Salvachúa,Eric M. Karp,Claire T. Nimlos,Derek R. Vardon,Derek R. Vardon,Gregg T. Beckham +5 more
TL;DR: The ability of 14 bacteria to secrete ligninolytic enzymes, depolymerize lignin, uptake aromatic and other compounds present in a biomass-derived, lign in-enriched stream, and, under nitrogen-limiting conditions, accumulate intracellular carbon storage compounds that can be used as fuel, chemical, or material precursors is examined.
Journal ArticleDOI
Degradation of Synthetic Azo Dyes of Textile Industry: a Sustainable Approach Using Microbial Enzymes
TL;DR: In this paper, the authors present an illustrated compilation of the use of microbial enzymes in removal of textile dyes, viz. laccase and azoreductase, which are cost-efficient, easy to harvest, easily downstream processable, and effortlessly mobilizable.
Journal ArticleDOI
Degradation of Anthraquinone Dyes from Effluents: A Review Focusing on Enzymatic Dye Degradation with Industrial Potential
TL;DR: Attention should be given to the emerging routes for dye decolorization via the enzymatic action of oxidoreductases, which have already a strong presence in various other bioremediation applications.
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