<abstract xml:lang="en" xmlns="http://www.w3.org/1999/xhtml">The optimal methodology to prepare the novel modified enzyme, polymer-enzyme complex, was developed to give a high catalytic activity in aqueous solution. The non-covalent complexes of two different enzymes (horseradish peroxidase and glucose oxidase) were prepared with various molar ratios (nD/nE 0,05; 0,1; 1; 5; 10; 15; 20) by using 75kDa dextran. The thermal stabilities of the obtained complexes were evaluated with the activities determined at different temperatures (25, 30, 35, 40, 50, 60, 70, 80°C) applying 60 minutes incubation time for pH 7. The complexes with the molar ratio nD/nHRP: 10 and nD/nGOD: 5 showed the highest thermal stability. Its activity was very high (<italic>ca</italic>. 1,5-fold higher activity than pure enzyme for HRP-dextran complexes) and almost the same between applying one hour incubation time and without incubation, and could also be measured at high temperatures (70, 80 °C). We finally succeeded in preparing dextran-enzyme complexes which showed higher activity than pure enzyme in aqueos solution at all temperatures for pH 7. In addition, the mentioned complexes at pH 7 had very long storage lifetime compared to purified enzyme at +4 °C; which is considered as a good feature for the usage in practice.</abstract>

The optimal methodology to prepare the novel modified enzyme, polymer-enzyme complex, was developed to give a high catalytic activity in aqueous solution. The non-covalent complexes of two different enzymes (horseradish peroxidase and glucose oxidase) were prepared with various molar ratios (nD/nE 0,05; 0,1; 1; 5; 10; 15; 20) by using 75kDa dextran. The thermal stabilities of the obtained complexes were evaluated with the activities determined at different temperatures (25, 30, 35, 40, 50, 60, 70, 80°C) applying 60 minutes incubation time for pH 7. The complexes with the molar ratio nD/nHRP: 10 and nD/nGOD: 5 showed the highest thermal stability. Its activity was very high (ca. 1,5-fold higher activity than pure enzyme for HRP-dextran complexes) and almost the same between applying one hour incubation time and without incubation, and could also be measured at high temperatures (70, 80 °C). We finally succeeded in preparing dextran-enzyme complexes which showed higher activity than pure enzyme in aqueos solution at all temperatures for pH 7. In addition, the mentioned complexes at pH 7 had very long storage lifetime compared to purified enzyme at +4 °C; which is considered as a good feature for the usage in practice.

Improvement of enzyme stability via non-covalent complex formation with dextran against temperature and storage lifetime

Faculty of Arts and Sciences, Department of Chemistry, Yildiz Technical University, Davutpasa Campus 34210 Esenler, Istanbul/TURKEY

Faculty of Chemical and Metallurgical Engineering, Department of Bioengineering, Yildiz Technical University, Davutpasa Campus 34210 Esenler, Istanbul/TURKEY

Polish Journal of Chemical Technology

The optimal methodology to prepare the novel modified enzyme, polymer-enzyme complex, was developed to give a high catalytic activity in aqueous solution. The...

Improvement of enzyme stability via non-covalent complex formation with dextran against temperature and storage lifetime

Publié en ligne: 08 avr. 2010

Pages: 12 - 16

DOI: https://doi.org/10.2478/v10026-010-0003-4

Mots clés
Thermal stabilization, Complex, Enzyme, Dextran, storage lifetime

This content is open access.

Improvement of enzyme stability via non-covalent complex formation with dextran against temperature and storage lifetime

Publié en ligne: 08 avr. 2010

Pages: 12 - 16

DOI: https://doi.org/10.2478/v10026-010-0003-4

Mots clésThermal stabilization, Complex, Enzyme, Dextran, storage lifetime

This content is open access.

Mots clés
Thermal stabilization, Complex, Enzyme, Dextran, storage lifetime