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Immobilization of horseradish peroxidase onto Purolite (R) A109 and its anthraquinone dye biodegradation and detoxification potential

Authorized Users Only
2020
Authors
Šekuljica, Nataša
Jovanović, Jelena
Jakovetić Tanasković, Sonja
Ognjanović, Nevena
Gazikalović, Ivana
Knežević-Jugović, Zorica
Mijin, Dušan
Article (Published version)
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Abstract
Horseradish peroxidase (HRP) is a highly specific enzyme with great potential for use in the decolorization of synthetic dyes. A comprehensive study of HRP immobilization using various techniques such as adsorption and covalent immobilization on the novel carrier Purolite (R) A109 with a special focus on enzymatic decolorization and toxicity of artificially colored wastewater. The immobilized preparations with an activity of 156.21 +/- 1.41 U g(-1) and 85.71 +/- 1.62 U g(-1) after the HRP adsorption and covalent immobilization, respectively, were obtained. Stability and reusability of the immobilized preparations were also evaluated. A noteworthy decolorization level (similar to 90%) with immobilized HRP was achieved. Phytotoxicity testing using Mung bean seeds and acute toxicity assay with Artemia salina has confirmed the applicability of the obtained immobilized preparation in industrial wastewater plants for the treatment of colored wastewater.
Keywords:
biodegradation / horseradish peroxidase / immobilization / synthetic dyes / toxicity / wastewater
Source:
Biotechnology Progress, 2020, 36, 4
Publisher:
  • Wiley, Hoboken
Funding / projects:
  • Study of the Synthesis, Structure and Activity of Natural and Synthetic Organic Compounds (RS-172013)
  • Novel encapsulation and enzyme technologies for designing of new biocatalysts and biologically active compounds targeting enhancement of food quality, safety and competitiveness (RS-46010)

DOI: 10.1002/btpr.2991

ISSN: 8756-7938

PubMed: 32170846

WoS: 000521621100001

Scopus: 2-s2.0-85082310685
[ Google Scholar ]
11
8
URI
http://TechnoRep.tmf.bg.ac.rs/handle/123456789/4457
Collections
  • Radovi istraživača (Inovacioni centar) / Researchers’ publications (Innovation Centre)
  • Radovi istraživača / Researchers’ publications (TMF)
Institution/Community
Tehnološko-metalurški fakultet
TY  - JOUR
AU  - Šekuljica, Nataša
AU  - Jovanović, Jelena
AU  - Jakovetić Tanasković, Sonja
AU  - Ognjanović, Nevena
AU  - Gazikalović, Ivana
AU  - Knežević-Jugović, Zorica
AU  - Mijin, Dušan
PY  - 2020
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/4457
AB  - Horseradish peroxidase (HRP) is a highly specific enzyme with great potential for use in the decolorization of synthetic dyes. A comprehensive study of HRP immobilization using various techniques such as adsorption and covalent immobilization on the novel carrier Purolite (R) A109 with a special focus on enzymatic decolorization and toxicity of artificially colored wastewater. The immobilized preparations with an activity of 156.21 +/- 1.41 U g(-1) and 85.71 +/- 1.62 U g(-1) after the HRP adsorption and covalent immobilization, respectively, were obtained. Stability and reusability of the immobilized preparations were also evaluated. A noteworthy decolorization level (similar to 90%) with immobilized HRP was achieved. Phytotoxicity testing using Mung bean seeds and acute toxicity assay with Artemia salina has confirmed the applicability of the obtained immobilized preparation in industrial wastewater plants for the treatment of colored wastewater.
PB  - Wiley, Hoboken
T2  - Biotechnology Progress
T1  - Immobilization of horseradish peroxidase onto Purolite (R) A109 and its anthraquinone dye biodegradation and detoxification potential
IS  - 4
VL  - 36
DO  - 10.1002/btpr.2991
UR  - conv_6085
ER  - 
@article{
author = "Šekuljica, Nataša and Jovanović, Jelena and Jakovetić Tanasković, Sonja and Ognjanović, Nevena and Gazikalović, Ivana and Knežević-Jugović, Zorica and Mijin, Dušan",
year = "2020",
abstract = "Horseradish peroxidase (HRP) is a highly specific enzyme with great potential for use in the decolorization of synthetic dyes. A comprehensive study of HRP immobilization using various techniques such as adsorption and covalent immobilization on the novel carrier Purolite (R) A109 with a special focus on enzymatic decolorization and toxicity of artificially colored wastewater. The immobilized preparations with an activity of 156.21 +/- 1.41 U g(-1) and 85.71 +/- 1.62 U g(-1) after the HRP adsorption and covalent immobilization, respectively, were obtained. Stability and reusability of the immobilized preparations were also evaluated. A noteworthy decolorization level (similar to 90%) with immobilized HRP was achieved. Phytotoxicity testing using Mung bean seeds and acute toxicity assay with Artemia salina has confirmed the applicability of the obtained immobilized preparation in industrial wastewater plants for the treatment of colored wastewater.",
publisher = "Wiley, Hoboken",
journal = "Biotechnology Progress",
title = "Immobilization of horseradish peroxidase onto Purolite (R) A109 and its anthraquinone dye biodegradation and detoxification potential",
number = "4",
volume = "36",
doi = "10.1002/btpr.2991",
url = "conv_6085"
}
Šekuljica, N., Jovanović, J., Jakovetić Tanasković, S., Ognjanović, N., Gazikalović, I., Knežević-Jugović, Z.,& Mijin, D.. (2020). Immobilization of horseradish peroxidase onto Purolite (R) A109 and its anthraquinone dye biodegradation and detoxification potential. in Biotechnology Progress
Wiley, Hoboken., 36(4).
https://doi.org/10.1002/btpr.2991
conv_6085
Šekuljica N, Jovanović J, Jakovetić Tanasković S, Ognjanović N, Gazikalović I, Knežević-Jugović Z, Mijin D. Immobilization of horseradish peroxidase onto Purolite (R) A109 and its anthraquinone dye biodegradation and detoxification potential. in Biotechnology Progress. 2020;36(4).
doi:10.1002/btpr.2991
conv_6085 .
Šekuljica, Nataša, Jovanović, Jelena, Jakovetić Tanasković, Sonja, Ognjanović, Nevena, Gazikalović, Ivana, Knežević-Jugović, Zorica, Mijin, Dušan, "Immobilization of horseradish peroxidase onto Purolite (R) A109 and its anthraquinone dye biodegradation and detoxification potential" in Biotechnology Progress, 36, no. 4 (2020),
https://doi.org/10.1002/btpr.2991 .,
conv_6085 .

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