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Peer-reviewedCC BY 4.0International Journal of Molecular Sciences

Enzymatic Degradation of the Textile Dye Remazol Brilliant Blue R, a Model Recalcitrant Anthraquinone Dye

  1. 1Amrita School of Biotechnology, Amrita Vishwa Vidyapeetham, Kollam 690525, Kerala, India
  2. 2Institute for Water and Wastewater Technology (IWWT), Durban University of Technology (DUT), Steve Biko Campus, Durban 4000, South Africa

Abstract

The massive discharge of Remazol Brilliant Blue R (RBBR), a recalcitrant anthraquinone dye, is of great environmental and public health concern due to its persistence, toxicity, and resistance to conventional wastewater treatment technologies. Enzymatic biodegradation has been developed as a sustainable alternative due to its high substrate specificity, mild operating conditions, and reduced secondary pollution. The review critically analyses the catalytic mechanisms, degradation pathways, and bioremediation potential of laccases, peroxidases, and azoreductases in degrading RBBR. Unlike azo dyes, RBBR lacks an azo (–N=N–) linkage; therefore, oxidative enzymes, particularly laccases and peroxidases, constitute the primary catalytic systems responsible for anthraquinone chromophore oxidation, whereas the contribution of azoreductases appears to be complementary and dependent on enzyme specificity and microbial metabolic interactions. Recent experimental evidence obtained using UV–Vis spectroscopy, Fourier-transform infrared spectroscopy (FTIR), High-performance liquid chromatography (HPLC), Liquid chromatography–mass spectrometry (LC–MS), Gas chromatography–mass spectrometry (GC–MS), enzyme assays, and phytotoxicity analyses has considerably improved understanding of RBBR degradation mechanisms and intermediate metabolite formation. The review also compares the catalytic efficiencies, advantages, and limitations of the three enzyme systems. Recent advances in enzyme immobilization, protein engineering, microbial consortia, and hybrid biotechnological approaches to improve degradation efficiency and operational stability are discussed. Finally, future perspectives on omics-assisted enzyme discovery, advanced metabolomic characterization, pilot-scale validation, and integrated treatment technologies are outlined to facilitate the development of efficient, scalable, and environmentally sustainable strategies for the remediation of anthraquinone dye-contaminated wastewater.

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BibTeX
@article{mahesh2026enzymatic,
  title = {{Enzymatic Degradation of the Textile Dye Remazol Brilliant Blue R, a Model Recalcitrant Anthraquinone Dye}},
  author = {Pala Mahesh and Noel Biju Longhinos and Nagabalaji Velmurugan and Bipin Gopalakrishnan Nair and Sanjay Pal and Suja Subhash},
  journal = {International Journal of Molecular Sciences},
  year = {2026},
  month = nov,
  doi = {10.3390/ijms27219982},
  url = {https://www.mdpi.com/1422-0067/27/21/9982},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Enzymatic Degradation of the Textile Dye Remazol Brilliant Blue R, a Model Recalcitrant Anthraquinone Dye
AU  - Pala Mahesh
AU  - Noel Biju Longhinos
AU  - Nagabalaji Velmurugan
AU  - Bipin Gopalakrishnan Nair
AU  - Sanjay Pal
AU  - Suja Subhash
PY  - 2026
DA  - 2026/11/07
JO  - International Journal of Molecular Sciences
DO  - 10.3390/ijms27219982
UR  - https://www.mdpi.com/1422-0067/27/21/9982
AB  - The massive discharge of Remazol Brilliant Blue R (RBBR), a recalcitrant anthraquinone dye, is of great environmental and public health concern due to its persistence, toxicity, and resistance to conventional wastewater treatment technologies. Enzymatic biodegradation has been developed as a sustainable alternative due to its high substrate specificity, mild operating conditions, and reduced secondary pollution. The review critically analyses the catalytic mechanisms, degradation pathways, and bioremediation potential of laccases, peroxidases, and azoreductases in degrading RBBR. Unlike azo dyes, RBBR lacks an azo (–N=N–) linkage; therefore, oxidative enzymes, particularly laccases and peroxidases, constitute the primary catalytic systems responsible for anthraquinone chromophore oxidation, whereas the contribution of azoreductases appears to be complementary and dependent on enzyme specificity and microbial metabolic interactions. Recent experimental evidence obtained using UV–Vis spectroscopy, Fourier-transform infrared spectroscopy (FTIR), High-performance liquid chromatography (HPLC), Liquid chromatography–mass spectrometry (LC–MS), Gas chromatography–mass spectrometry (GC–MS), enzyme assays, and phytotoxicity analyses has considerably improved understanding of RBBR degradation mechanisms and intermediate metabolite formation. The review also compares the catalytic efficiencies, advantages, and limitations of the three enzyme systems. Recent advances in enzyme immobilization, protein engineering, microbial consortia, and hybrid biotechnological approaches to improve degradation efficiency and operational stability are discussed. Finally, future perspectives on omics-assisted enzyme discovery, advanced metabolomic characterization, pilot-scale validation, and integrated treatment technologies are outlined to facilitate the development of efficient, scalable, and environmentally sustainable strategies for the remediation of anthraquinone dye-contaminated wastewater.
SN  - 1422-0067
ER  -