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<p>Synthetic azo dyes are the commonly utilized colorants in various food products, and textile industries, however, their adverse cytotoxicity and carcinogenicity are the major concern. Laccase is a promising approach for azo dyes degradation, nevertheless, its availability and catalytic versatility is the challenge, thus, purification of this enzyme from the fungi grown on agriculture residues was the objective. <i>Aspergillus oryzae</i> PZ027891, was the highest laccase producer (45&#xa0;μmol/mg/min), grown on peanut peels under solid state conditions. The enzyme was partially purified from <i>A. oryzae</i> by 1.3 folds by ultracentrifugation and gel-filtration chromatography, with subunit structure 65&#xa0;kDa. <i>A. oryzae</i> laccase was immobilized on sodium alginate (SA-AoLacc), with immobilization yield 82.5%. At 40&#xa0;°C, SA-AoLacc composite has a plausible thermal stability by 2 folds increments, compared to native one. From the SEM–EDX analysis, the SA-Aolacc beads surface were extensively heterogeneous, uneven textured, with an obvious increase to the elemental composition of oxygen and copper, ensuring the dispersion and entrapment of this enzyme within the gel beads. The SA-Aolacc composite beads have the ability to de-colorize the azo dye by 94.7%, after 3&#xa0;h contact time, using the natural lignin oxidative products as intrinsic mediator. From the LC/MS analysis, the intensity of azo dye (327.3&#xa0;m/z) was strongly reduced by 98.8%, with emergence of molecular fragments of 124.06, 136.1, and 289.1&#xa0;m<i>/z</i>, ensuring the asymmetric degradation of dye. The SA-Aolacc composite retains 50% of its initial activity by the 5th cycle, ensuring their economical affordability to be a platform for azo dye degradation.</p>

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Sodium alginate–entrapped laccase from solid-state cultures of Aspergillus oryzae as a promising system for asymmetric degradation of synthetic azo dyes

  • 期刊论文

  • 发表日期：

    2026年7月30日

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  • Hala N. Elghamry,
  • Mohamed G. Seadawy,
  • Abdurrahman S. Masrahi,
  • Samar A. Khashana,
  • Ashraf S. A. El-Sayed

摘要

Synthetic azo dyes are the commonly utilized colorants in various food products, and textile industries, however, their adverse cytotoxicity and carcinogenicity are the major concern. Laccase is a promising approach for azo dyes degradation, nevertheless, its availability and catalytic versatility is the challenge, thus, purification of this enzyme from the fungi grown on agriculture residues was the objective. Aspergillus oryzae PZ027891, was the highest laccase producer (45 μmol/mg/min), grown on peanut peels under solid state conditions. The enzyme was partially purified from A. oryzae by 1.3 folds by ultracentrifugation and gel-filtration chromatography, with subunit structure 65 kDa. A. oryzae laccase was immobilized on sodium alginate (SA-AoLacc), with immobilization yield 82.5%. At 40 °C, SA-AoLacc composite has a plausible thermal stability by 2 folds increments, compared to native one. From the SEM–EDX analysis, the SA-Aolacc beads surface were extensively heterogeneous, uneven textured, with an obvious increase to the elemental composition of oxygen and copper, ensuring the dispersion and entrapment of this enzyme within the gel beads. The SA-Aolacc composite beads have the ability to de-colorize the azo dye by 94.7%, after 3 h contact time, using the natural lignin oxidative products as intrinsic mediator. From the LC/MS analysis, the intensity of azo dye (327.3 m/z) was strongly reduced by 98.8%, with emergence of molecular fragments of 124.06, 136.1, and 289.1 m/z, ensuring the asymmetric degradation of dye. The SA-Aolacc composite retains 50% of its initial activity by the 5th cycle, ensuring their economical affordability to be a platform for azo dye degradation.