Journals / Tekstil ve Konfeksiyon / 2021 / Cilt: 31 - Sayı: 1

Experimental Design Optimization and Decolorization of an Azo Dye by Cross-Linked Peroxidase Aggregates

Pages
34–42
Publication Date
2021-03-31
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

Under optimal conditions, a textile azo dye, Reactive Blue 160 was completely oxidized within 90 h and higher temperatures also showed promising results in dye degradation.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:The immobilization of horseradish peroxidase in the form of cross-linked enzyme aggregates (HRP–CLEAs) was optimized by three parameters full factorial experimental design at two levels and the degradation of an azo dye was tested.
📊
Key Findings & Data:The optimal immobilization conditions were estimated as 0.06 mg enzyme/mL (0.96 U), 3 % (v/v, Glutaraldehyde)) cross-linker ratio, and 6 mg /mL Bovine Serume Albumine amount, respectively.
💡
Conclusion & Impact:Under optimal conditions, a textile azo dye, Reactive Blue 160 was completely oxidized within 90 h and higher temperatures also showed promising results in dye degradation.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Cross-Linked Enzyme Aggregates (CLEAs) · Horseradish Peroxidase · Full Factorial Design

Abstract

The immobilization of horseradish peroxidase in the form of cross-linked enzyme aggregates (HRP–CLEAs) was optimized by three parameters full factorial experimental design at two levels and the degradation of an azo dye was tested. The optimal immobilization conditions were estimated as 0.06 mg enzyme/mL (0.96 U), 3 % (v/v, Glutaraldehyde)) cross-linker ratio, and 6 mg /mL Bovine Serume Albumine amount, respectively. The effects of variables were analysed by responce surface plots and the enzyme concentration effect was insignificant for the tested levels. The maximum CLEAs activity was 0.2188 U and the kinetic parameters (Km and Vmax) were 0.0314 mM and 0.1044 mM/min while the calculated values for soluble enzyme were 0.06 mM and 0.468 mM/min, respectively. Hydrogen peroxide has inhibitory effect on enzyme aggregate activities at higher amounts than 0.012 mM. Under optimal conditions, a textile azo dye, Reactive Blue 160 was completely oxidized within 90 h and higher temperatures also showed promising results in dye degradation.

🔖

Cite This Article

AYHAN, F., AKPOLAT, O. (2021). Experimental Design Optimization and Decolorization of an Azo Dye by Cross-Linked Peroxidase Aggregates. Tekstil ve Konfeksiyon, Cilt: 31 - Sayı: 1, 34–42. https://ajindex.com/articles/219215

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (3)

  1. Da Silva M. R., de Sà, L. R. V., Russo C., Scio E. Ferreira-Leitao V. S., Volume 2010, The Use of HRP in Decolorization of Reactive Dyes and Toxicological Evaluation of Their Products. SAGE-Hindawi Access to Research Enzyme Research, Article ID 703824, 7 pages http://dx.doi.org/10.4061/2010/703824.2.
  2. Levin L., Forchiassin F., Viale A., 2005, Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements. Process Biochemistry, 40, pp: 1381–1387. https://doi.org/10.1002/1521-3846(200105)21:2 3.0.CO;2-2.3. Shaheen, R., Asghera M., Hussaina F., Bhatti H. N., 2017, Immobilized lignin peroxidase from Ganoderma lucidum IBL-05 with improved dye decolorization and cytotoxicity reduction properties. International Journal of Biological Macromolecules 103, pp: 57–64. https://doi.org/10.1016/j.ijbiomac.2017.04.040. 4. Robinson T., McMullan G., Marchant R. Nigam P., 2001, Remediation of dyes in textile effluent: a critical review on current treatment technologies with a proposed alternative. Bioresource Technology, 77, pp: 247-255. https://doi.org/10.1016/S0960-8524(00)00080-8.5.
  3. Rathnamsamy S. Singh R., Auxilia R., Vedhahari B.N., 2014, Extraction of peroxidasese from various plant sources and its biodegradation studies on phenolic compounds. BioTechnology, 9(4), pp: 160-165. 6. Pandey V. P., Awasthi M., Singh, S. Tiwari S., Dwivedi U. N., 2017, A Comprehensive Review on Function and Application of Plant Peroxidases. Biochem Anal Biochem 6, pp: 1-16. doi:10.4172/2161-1009.10003087. Kawakita H., 2012, Metal Recovery Using Polyphenols Prepared by Enzymatic Reactions of Horseradish Peroxidase. Science and Technology, 2 (1), pp:25-29 DOI: 10.5923/j.scit.20120201.05 8. Kariminiaae-Hamedaani H-R. Sakurai A. Sakakibara M., 2007, Decolorization of synthetic dyes by a new manganese peroxidase producing white rot fungus. Dyes Pigments, 72, pp: 157-162. doi:10.1016/j.dyepig.2005.08.010. 9. Hamad I. S. Ahmed A., Azim A., 2013, Biodegradation of phenols in wastewater using crude peroxidases five weed plants. J Chem & Pharmac R., 5 (4), pp: 60. 10. Bansal P., Dhir A., Prakash N. T., Sud D., July 2011, Environmental remediation of wastewater containing azo dyes with a heterostructured nanophotocatalyst. Indian Journal of Chemistry Vol. 50A, pp. 991-995. 11. Farias S., de Oliveira D., Ulson de Souza, A. A., Guelli S. M. A., de Souza U., Morgado A. F., 2017, Removal of reactıve blu