ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2025
Kraft lignin biobleaching by a dye-decolorizing peroxidase from the Antarctic Pseudomonas sp. AU10 strain.
Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Dye-Decolorizing Peroxidase for Lignin Depolymerization: a Comprehensive Review on Enzyme Structural Characteristics, Reaction-Influencing Factors and Efficiency-Enhancing Strategies.Applied biochemistry and biotechnology · 2026Review
- Dye-Decolorizing Peroxidase for Lignin Depolymerization: a Comprehensive Review on Enzyme Structural Characteristics, Reaction-Influencing Factors and Efficiency-Enhancing Strategies.Applied biochemistry and biotechnology · 2026Review
- Optimization and comparative evaluation of fungal laccase-based biobleaching of pineapple leaf pulp: toward sustainable non-wood pulp processing using Paramarasmius palmivorus.Biotechnology letters · 2026Article
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3 authors.
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Abstract
Pseudomonas sp. AU10 is an Antarctic psychrotolerant bacterium that produces a dye-decolorizing peroxidase (DyP-AU10). The recombinant enzyme (rDyP-AU10) is a heme-peroxidase that decolors dyes and modifies kraft lignin. In this work, we report the best activity parameters for lignin modification (at 45 °C and pH 4) and show that the enzyme increases the number of aldehydes, ketones, and phenolic compounds. The analyses of the HPLC profile of samples also support that rDyP-AU10 induces the chemical change of kraft lignin. The enzyme also acts as a biobleaching agent on cellulose pulps, as shown by the reduction in kappa number. We also included experiments with a commercial laccase from Trametes versicolor and performed experiments using single enzymes and, in combination. The results show that rDyP-AU10 and the commercial laccase do not have a synergic activity as a modifying system, on cellulose pulp as substrates. However, results suggest that rDyP-AU10 holds potential as a member of the portfolio of lignin-modifying enzymes.
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