The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Tailor-made biocatalysts based on scarcely studied acidic horseradish peroxidase for biodegradation of reactive dyes
Abstract
Peroxidases (EC 1.11.1.7) have enormous biotechnological applications. Usage of more abundant, basic isoforms of peroxidases in diagnostic kits and/or in immunochemistry has led to under exploitation and disregard of horseradish peroxidase (HRP) acidic isoforms. Therefore, acidic horseradish peroxidase (HRP-A) isoenzyme was used for the preparation of a biocatalyst with improved ability in dye decolorization. Ten biocatalysts were prepared by covalent binding of enzyme to chitosan and alginate, adsorption followed by cross-linking on inorganic support (aluminum oxide), and encapsulation in spherical calcium alginate beads via polyethylene glycol. Model dyes of 50 to 175 mg l -1 were removed by the biocatalysts. Among the tested biocatalysts, the three with the highest specific activity and biodegradation rate were further studied (Chitosan-HRP, Al-Gel-HRP and Al-HRP-Gel). The impact of hydrogen peroxide concentration on dye decolorization was examined on the Chitosan-HRP biocatalyst, since the HRP is susceptible to inhibition/inactivation by high H 2 O 2 . On the other hand, H 2 O 2 is needed as a co-substrate for the HRP, and the H 2 O 2 /dye ratio can greatly influence decolorization efficiency. Concentrations of H 2 O 2 ranging from 0.22 to 4.4 mM showed no difference in terms of impact on the biocatalyst decolorization efficiency. The high decolorization efficiency of the biocatalysts was validated by the removal of 25 and 100 mg l -1 anthraquinone (Remazol Brilliant Blue…
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“Majority of examples examined are using lengthy synthesis procedures with many subsequent steps for the materials synthesis and the immobilisation of the enzyme, and further hazardous chemicals and unsustainable practices are usually employed 189, 192, 196, 197, 199, 222-224 .”
From Degradation of anthraquinone dyes from effluents: A review focusing on enzymatic dye degradation with industrial potential (2020) · cites this paper as [196]
Citations
Cites
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Improvement of enzyme activity, stability and selectivity via immobilization techniques
Mateo, C., Palomo, J. M., Fernandez-Lorente, G., Guisan, J. M., & Fernandez-Lafuente, R. (2007) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2007.01.018 · Cited by 3,375
Enzyme Immobilization: The Quest for Optimum Performance
Sheldon, R. A. (2007) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.200700082 · Cited by 2,077
Biodegradation of Synthetic Dyes—A Review
Ali, H. (2010) · Water, Air, & Soil Pollution · doi:10.1007/s11270-010-0382-4 · Cited by 817
(2012) · doi:10.5772/32373 · Cited by 640
Oxidation of sodium alginate and characterization of the oxidized derivatives
Gomez, C. G., Rinaudo, M., & Villar, M. A. (2007) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2006.05.025 · Cited by 441
Principles, techniques, and applications of biocatalyst immobilization for industrial application
Eş, I., Vieira, J. D. G., & Amaral, A. C. (2015) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-015-6390-y · Cited by 388
Suicide Inactivation of Peroxidases and the Challenge of Engineering More Robust Enzymes
Valderrama, B., Ayala, M., & Vazquez-Duhalt, R. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00149-7 · Cited by 366
An updated view on horseradish peroxidases: recombinant production and biotechnological applications
Krainer, F., & Glieder, A. (2015) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-6346-7 · Cited by 242
Kinetics of the adsorption of reactive dyes by chitin
Akkaya, G., Uzun, İ., & Güzel, F. (2006) · Dyes and Pigments · doi:10.1016/j.dyepig.2005.11.005 · Cited by 218
Cited by
Routoula, E., & Patwardhan, S. V. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.9b03737 · Cited by 579
Metadata
- Authors
- Janović, B. S., Mićić Vićovac, M. L., Vujčić, Z. M., & Vujčić, M. T.
- Venue
- Environmental Science and Pollution Research
- Published
- 2016-12-01
- Volume
- 24
- Issue
- 4
- Pages
- 3923-3933
- ISSN
- 0944-1344
- 1614-7499
- Cited by
- 16
- References
- 45
- Language
- en
- Funders
- Ministarstvo Prosvete, Nauke i Tehnološkog Razvoja (172048)
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