Title of article :
Immobilization of catalase via adsorption onto l-histidine grafted functional pHEMA based membrane
Author/Authors :
Akgِl، نويسنده , , Sinan and Kaçar، نويسنده , , Yasemin and ضzkara، نويسنده , , Serpil and Yavuz، نويسنده , , Handan and Denizli، نويسنده , , Adil and Arica، نويسنده , , M.Yakup، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2001
Abstract :
Poly(2-hydroxyethylmethacrylate) (pHEMA) based flat sheet membrane was prepared by UV-initiated photopolymerization technique. The membrane was then grafted with l-histidine. Catalase immobilization onto the membrane from aqueous solutions containing different amounts of catalase at different pH was investigated in a batch system. The maximum catalase immobilization capacity of the pHEMA–histidine membrane was 86 μg cm−2. The activity yield was decreased with the increase of the enzyme loading. It was observed that there was a significant change between Vmax value of the free catalase and Vmax value of the adsorbed catalase on the pHEMA–histidine membrane. The Km value of the immobilized enzyme was higher 1.5 times than that of the free enzyme. Optimum operational temperature was 5°C higher than that of the free enzyme and was significantly broader. It was observed that enzyme could be repeatedly adsorbed and desorbed without loss of adsorption capacity or enzyme activity.
Keywords :
Immobilization , pHEMA membrane , Adsorption , L-histidine , Catalase
Journal title :
Journal of Molecular Catalysis B Enzymatic
Journal title :
Journal of Molecular Catalysis B Enzymatic