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Article 2025 · 4 citations

Decolorization of Azo and Anthraquinone Dyes Using Recombinant Horseradish Peroxidase A2A Isoenzyme Produced by <i>Komagataella phaffii</i>

Abul, Nurgul, Arslan, Seyda Yildiz, Unver, Yagmur, Ozdemir, Hasan

Abstract

Water pollution is a significant issue due to industrialization and population growth, and one of the main sources of wastewater is synthetic dyes. The textile sector is particularly affected by dyes like azo and anthraquinone dyes, which are difficult to degrade and produce toxic organic waste. Currently, synthetic dyes are processed through physical and chemical methods, which have financial and methodological disadvantages. Horseradish peroxidase (HRP) is a widely studied enzyme for purifying pollutants like dyes and phenols in wastewater. However, their high cost makes them a costly option. Recombinant protein production is suitable for the mass production of stable and resistant enzymes. In this study, the decolorization potential of recombinant HRP A2A (rHRP A2A) isoenzyme secreted by Komagataella phaffii and purified by affinity technique in a single step on Acid blue 113, Alizarin red, and Remazol brilliant blue R was presented for the first time, and the optimal conditions for the highest decolorization rate were determined. Fe2+ and Mn2+ metal ions increased enzyme activity by 158.62% and 79.54%, respectively. Color removal with 0.006 EU/mL rHRP A2A for Acid blue 113, Alizarin red, and Remazol brilliant blue R was observed at 71.27, 62.26, and 31.22%, respectively. ABTS served as a redox mediator, significantly increasing the rate of dye decolorization in a shorter period at the specified concentration.

Keywords
Recombinant HRP A2A isoenzyme Azo dye Anthraquinone dye Decolorization Water pollution ENZYMATIC DECOLORIZATION METHYLENE-BLUE PURIFICATION DEGRADATION OXIDATION TEXTILE INHIBITION L. DETOXIFICATION OPTIMIZATION
WoS Categories
Biochemistry & Molecular Biology Biotechnology & Applied Microbiology
Sustainable Development Goals
Citation
Journal
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
Year
2025
Volume
197
Issue
7
Pages
4547-4564
ISSN
0273-2289
eISSN
1559-0291
DOI
10.1007/s12010-025-05239-8
WoS UID
WOS:001480462100001
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