β-galactosidase immobilization into poly(hydroxyethyl methacrylate) membrane and performance in a continuous system
Yükleniyor...
Tarih
1999
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Wiley-Blackwell
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
The activity of beta-galactosidase immobilized into a poly(2-hydroxyethyl methacrylate) (pHEMA) membrane increased from 1.5 to 10.8 U/g pHEMA upon increase in enzyme loading. The K-m values for the free and the entrapped enzyme were found to be 0.26 and 0.81 mM, respectively. The optimum reaction temperatures for the free and the entrapped beta-galactosidase were both found to be 50 degrees C. Similarly, the optimum reaction pH was 7.5 for both the free and the entrapped enzyme. The immobilized beta-galactosidase was characterized in a continuous system during lactose hydrolysis and the operational inactivation rate constant (k(iop)) of the entrapped enzyme was found to be 3.1 x 10(-5) min(-1). (C) 1999 John Wiley & Sons, Inc.
Açıklama
Baran, Erkan/0000-0002-0563-6943; Baran, Erkan/0000-0002-0563-6943;
Anahtar Kelimeler
beta-galactosidase, enzyme immobilization, pHEMA, lactose hydrolysis, enzyme-membrane reactor
Kaynak
Journal Of Applied Polymer Science
WoS Q Değeri
Q2
Scopus Q Değeri
Q2
Cilt
72
Sayı
10
Künye
closedAccess
