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

• Autorzy: Altikatoglu M. , Kuzu H.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

thermal stabilization; complex; enzyme; dextran; storage lifetime

PL

stabilizacja termiczna; enzymy; dekstran

• Wydawca: West Pomeranian University of Technology. Publishing House
• Czasopismo: Polish Journal of Chemical Technology
• Rocznik: 2010
• Tom: Vol. 12, nr 1
• Strony: 12--16
• Opis fizyczny: Bibliogr. 35 poz., rys.

Twórcy

autor

Altikatoglu M.

autor

Kuzu H.

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

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