<abstract xmlns="http://www.w3.org/1999/xhtml">The thermal stability of enzyme-based biosensors is crucial in economic feasibility. In this study, thermal deactivation profiles of catalase <italic>Aspergillus niger</italic> were obtained at different temperatures in the range of 35°C to 70°C. It has been shown that the thermal deactivation of catalase <italic>Aspergillus niger</italic> follows the first-order model. The half-life time <italic>t</italic>1/2 of catalase <italic>Aspergillus niger</italic> at pH 7.0 and the temperature of 35°C and 70°C were 197 h and 1.3 h respectively. Additionally, <italic>t</italic>1/2 of catalase <italic>Aspergillus niger</italic> at the temperature of 5°C was calculated 58 months. Thermodynamic parameters the change in enthalpy <italic>ΔH</italic>*, the change in entropy <italic>ΔS</italic>* and the change Gibbs free energy <italic>ΔG</italic>* for the deactivation of catalase at different temperatures in the range of 35°C to 70°C were estimated. Catalase <italic>Aspergillus niger</italic> is predisposed to be used in biosensors by thermodynamics parameters obtained.</abstract>

The thermal stability of enzyme-based biosensors is crucial in economic feasibility. In this study, thermal deactivation profiles of catalase Aspergillus niger were obtained at different temperatures in the range of 35°C to 70°C. It has been shown that the thermal deactivation of catalase Aspergillus niger follows the first-order model. The half-life time t1/2 of catalase Aspergillus niger at pH 7.0 and the temperature of 35°C and 70°C were 197 h and 1.3 h respectively. Additionally, t1/2 of catalase Aspergillus niger at the temperature of 5°C was calculated 58 months. Thermodynamic parameters the change in enthalpy ΔH*, the change in entropy ΔS* and the change Gibbs free energy ΔG* for the deactivation of catalase at different temperatures in the range of 35°C to 70°C were estimated. Catalase Aspergillus niger is predisposed to be used in biosensors by thermodynamics parameters obtained.

Thermodynamics and kinetics of thermal deactivation of catalase <italic>Aspergillus niger</italic>

Department of Chemical and Biochemical Engineering, Faculty of Chemical Technology and Engineering

University of Science and Technology Bydgoszcz

Polish Journal of Chemical Technology

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Thermodynamics and kinetics of thermal deactivation of catalase 

The thermal stability of enzyme-based biosensors is crucial in economic feasibility. In this study, thermal deactivation profiles of catalase Aspergillus niger...

Thermodynamics and kinetics of thermal deactivation of catalase Aspergillus niger

Online veröffentlicht: 13. Mai 2020

Seitenbereich: 67 - 72

DOI: https://doi.org/10.2478/pjct-2020-0018

Schlüsselwörter
catalase, thermal deactivation, thermodynamics parameters, hydrogen peroxide

© 2020 Justyna Miłek, published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Thermodynamics and kinetics of thermal deactivation of catalase Aspergillus niger

Online veröffentlicht: 13. Mai 2020

Seitenbereich: 67 - 72

DOI: https://doi.org/10.2478/pjct-2020-0018

Schlüsselwörtercatalase, thermal deactivation, thermodynamics parameters, hydrogen peroxide

© 2020 Justyna Miłek, published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Schlüsselwörter
catalase, thermal deactivation, thermodynamics parameters, hydrogen peroxide