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Vol 9, Issue 1, 2025
Pages: 34 -
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Abstract Environment

COVALENT IMMOBILIZATION OF HORSERADISH PEROXIDASE ON BIO-LINKED MAGNETITE NANOPARTICLES

By
Mirjana Petronijević ,
Mirjana Petronijević
Contact Mirjana Petronijević

University of Novi Sad, Faculty of Technology Novi Sad, Bulevar cara Lazara 1 , Novi Sad , Serbia

Sanja Panić ,
Sanja Panić

University of Novi Sad, Faculty of Technology Novi Sad, Bulevar cara Lazara 1 , Novi Sad , Serbia

Aleksandra Cvetanović Kljakić ,
Aleksandra Cvetanović Kljakić

University of Novi Sad, Faculty of Technology Novi Sad, Bulevar cara Lazara 1 , Novi Sad , Serbia

Biljana Lončar ,
Biljana Lončar

University of Novi Sad, Faculty of Technology Novi Sad, Bulevar cara Lazara 1 , Novi Sad , Serbia

Jelena Tanasić ,
Jelena Tanasić

University of Novi Sad, Faculty of Technology Novi Sad, Bulevar cara Lazara 1 , Novi Sad , Serbia

Jelena Arsenijević ,
Jelena Arsenijević

University of Belgrade, Faculty of Pharmacy, Vojvode Stepe 450 , Belgrade , Serbia

Slavica Ražić
Slavica Ražić

University of Belgrade, Faculty of Pharmacy, Vojvode Stepe 450 , Belgrade , Serbia

Abstract

Enzymes, such as peroxidases, are “green” catalysts used in various environmental processes. Enzymes can be used in free form or immobilized on a solid support such as metal oxides, carbon and composite materials. The appropriate choice of carrier can significantly improve the properties of the enzyme, increase its stability and enable its reuse in multiple cycles.

In this work, the suitability of bio-linked magnetite particles as a solid support for the immobilization of horseradish peroxidase was investigated. The magnetite particles were synthesized by the co-precipitation method in the presence of subcritical water extracts from tangerine peels. The extraction was carried out at 140°C and autogenous pressure for 10 minutes. The synthesized bio-linked magnetite particles were used as carriers for the immobilization of peroxidase over glutaraldehyde. First, the magnetite particles were modified by mixing with 1% glutaraldehyde for 6 hours to attach functional groups suitable for covalent binding of the enzyme to the surface of the magnetite. Subsequently, the commercial horseradish peroxidase was covalently bound to the modified magnetite particles via aldehyde groups. The resulting biocatalyst showed high enzymatic activity (65 U/g). The biocatalyst retains its high activity in the pH range of 6-8 and in the temperature range 40-60°C. It can be concluded that the synthesized biocatalyst has the potential to be used in various environmental applications.  

 

Funding Statement

This research was supported by the Science Fund of the Republic of Serbia, #GRANT No 7464, Novel Bio-linked Magnetite/geopolymer Composites in Phenol-containing Wastewater Treatment: Toward Zero-waste Technology - BioCompWaterClean.

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