Immobilization of catalase via adsorption onto L-histidine grafted functional pHEMA based membrane

AKGOL, HANDAN; KACAR, Y; OZKARA, S; Yavuz, HANDAN; DENIZLI, ADİL; ARICA, MY

doi:10.1016/s1381-1177(01)00029-7

Immobilization of catalase via adsorption onto L-histidine grafted functional pHEMA based membrane

Atıf İçin Kopyala

AKGOL S., KACAR Y., OZKARA S., Yavuz H., DENIZLI A., ARICA M.

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, cilt.15, ss.197-206, 2001 (SCI-Expanded)

Yayın Türü: Makale / Tam Makale
Cilt numarası: 15
Basım Tarihi: 2001
Doi Numarası: 10.1016/s1381-1177(01)00029-7
Dergi Adı: JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
Sayfa Sayıları: ss.197-206
Hacettepe Üniversitesi Adresli: Evet

Özet

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 mug cm(-2). The activity yield was decreased with the increase of the enzyme loading. It was observed that there was a significant change between V-max value of the free catalase and V-max value of the adsorbed catalase on the pHEMA-histidine membrane. The K-m value of the immobilized enzyme was higher 1.5 times than that of the free enzyme. Optimum operational temperature was 5 degreesC 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. (C) 2001 Elsevier Science B.V. All rights reserved.