journal article·2024-03-13Open access

The Energies of Activation and Deactivation of 2,4-Dichlorophenol Degradation by Horseradish Peroxidase Immobilized on the Modified Nanofibrous Membrane

Justyna Miłek

Applied Sciences· Volume 14· Issue 6

Abstract

Chlorophenol compounds pose a health risk to many organisms due to their toxicity. The present paper presents the estimation of the activation and deactivation energies and the optimum temperatures of 2,4-dichlorophenol degradation by horseradish peroxidase (HRP). The activities of horseradish peroxidase depending on temperature were analyzed. In a mathematical model, describing 2,4-dichlorophenol degradation by HRP was assumed that both the 2,4-dichlorophenol degradation and the deactivation of HRP were first-order reactions by the enzyme concentration. The parameters of the optimum temperatures Topt, the activation energies Er, and the deactivation energies Ed in the process of 2,4-dichlorophenol degradation by HRP immobilized on a modified nanofibrous membrane were determined kd and t1/2 were determined for HRP immobilized at temperatures in the range of 25 °C to 75 °C. Likewise, thermodynamic parameters such as the change in the enthalpy ∆H#, change in entropy ∆S#, the change in Gibbs free energy ∆G# for native HPR and the change in the enthalpy ∆Hd#, change in entropy ∆Sd#, and the change in Gibbs free energy ∆Gd# for deactivated HRP were determined at 25 °C.
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Research context

OpenAlex topics: Electrochemical sensors and biosensors · Enzyme Catalysis and Immobilization · Enzyme-mediated dye degradation

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Department of Chemical and Biochemical Engineering, Faculty of Chemical Technology and Engineering, Bydgoszcz University of Science and Technology, Seminaryjna 3, 85-324 Bydgoszcz, Poland

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