<p>Biological delignification by laccase offers cost-effectiveness, energy efficiency, and environmental benefits. In this context, extremophiles and extremozymes enhance biomass pretreatment and lignin depolymerization, showing superior performance under harsh conditions. This study focused on isolating and characterizing a polyextremophilic bacterial isolate, identified <i>Halomonas elongata</i>, demonstrating laccase production under extreme circumstances. The enzyme production was enhanced to 719 U L<sup>−1</sup> under the optimized conditions (pH 8.9, 1.5 M NaCl, 3.5 mM copper sulfate, and 1.58% w/v yeast extract). The extremozyme (183.4 U L<sup>−1</sup>), in combination with a 9.7 mM 1-hydroxybenzotriazole (HBT; as laccase mediator), effectively depolymerized lignin in pumpkin seed shells (30 mg mL<sup>−1</sup>) at 54.5 °C, obtaining a delignification efficiency of 95.1%. The enzymatic treatment significantly reduced lignin content (29.5 to 20.7%) while increasing cellulose accessibility (48.9 to 53.3%) in the biomass shells. Surface characterization using a scanning electron microscope (SEM) confirmed structural alterations in the biowaste, indicating successful lignin degradation. Gas chromatography-mass spectrometry (GC–MS) analysis of the byproducts revealed the formation of some valuable substances such as guaiacol, <i>o</i>-cresol, and ethyl 2-hydroxy-2-(4-hydroxyphenyl)acetate, providing insights into the bio-delignification pathway. This research demonstrates the promising potential of polyextremophilic laccases and enzymatic delignification for efficient and environmentally friendly depolymerization of lignocellulosic biomass.</p>

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In the pursuit of an efficient delignification from pumpkin seed shells by the polyextremophilic and laccase-producing bacterial isolate Halomonas elongata

  • Tina Adelpour,
  • Ahmad Reza Shahverdi,
  • Mohsen Amini,
  • Mohammad Ali Faramarzi,
  • Somayeh Mojtabavi

摘要

Biological delignification by laccase offers cost-effectiveness, energy efficiency, and environmental benefits. In this context, extremophiles and extremozymes enhance biomass pretreatment and lignin depolymerization, showing superior performance under harsh conditions. This study focused on isolating and characterizing a polyextremophilic bacterial isolate, identified Halomonas elongata, demonstrating laccase production under extreme circumstances. The enzyme production was enhanced to 719 U L−1 under the optimized conditions (pH 8.9, 1.5 M NaCl, 3.5 mM copper sulfate, and 1.58% w/v yeast extract). The extremozyme (183.4 U L−1), in combination with a 9.7 mM 1-hydroxybenzotriazole (HBT; as laccase mediator), effectively depolymerized lignin in pumpkin seed shells (30 mg mL−1) at 54.5 °C, obtaining a delignification efficiency of 95.1%. The enzymatic treatment significantly reduced lignin content (29.5 to 20.7%) while increasing cellulose accessibility (48.9 to 53.3%) in the biomass shells. Surface characterization using a scanning electron microscope (SEM) confirmed structural alterations in the biowaste, indicating successful lignin degradation. Gas chromatography-mass spectrometry (GC–MS) analysis of the byproducts revealed the formation of some valuable substances such as guaiacol, o-cresol, and ethyl 2-hydroxy-2-(4-hydroxyphenyl)acetate, providing insights into the bio-delignification pathway. This research demonstrates the promising potential of polyextremophilic laccases and enzymatic delignification for efficient and environmentally friendly depolymerization of lignocellulosic biomass.