Characterization of β-galactosidase immobilized into poly(hydroxyethylmethacrylate) membranes

[ X ]

Tarih

1998

Dergi Başlığı

Dergi ISSN

Cilt Başlığı

Yayıncı

Mbr Press Inc

Erişim Hakkı

info:eu-repo/semantics/closedAccess

Özet

beta-galactosidase was immobilized into pHEMA membranes with the highest specific activity yield of 9.5%. The specific activity of the entrapped enzyme was found to be decreased as the enzyme loading increased in pHEMA membranes. The optimum pH and temperature for maximum activity of the immobilized beta-galactosidase was found to be at pH 7.5 and 50 degrees C, respectively, and were the same as native enzyme. K-m and V-max values for the free enzyme were found to be 0.256 mM and 26.6 mu mole/min/mg, respectively. K-m value of immobilized beta-galactosidase was found to be increased about 3 folds upon immobilization. Operational, thermal and storage stability of beta-galactosidase were found to increase with immobilization. Immobilized enzyme preparation was reused in 15 cycles without significant loss in activity.

Açıklama

Baran, Erkan/0000-0002-0563-6943; Baran, Erkan/0000-0002-0563-6943

Anahtar Kelimeler

beta-galactosidase, immobilization

Kaynak

Biochemical Archives

WoS Q Değeri

Q4

Scopus Q Değeri

Cilt

14

Sayı

2

Künye

closedAccess