Premium
β‐Galactosidase immobilization into poly(hydroxyethyl methacrylate) membrane and performance in a continuous system
Author(s) -
Arica M. Yakup,
Baran Türker,
Denizli Adil
Publication year - 1999
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/(sici)1097-4628(19990606)72:10<1367::aid-app17>3.0.co;2-d
Subject(s) - methacrylate , 2 hydroxyethyl methacrylate , immobilized enzyme , hydrolysis , membrane , polymer chemistry , chemistry , (hydroxyethyl)methacrylate , lactose , enzyme , chromatography , chemical engineering , polymer , organic chemistry , polymerization , biochemistry , engineering
The activity of β‐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 m M, respectively. The optimum reaction temperatures for the free and the entrapped β‐galactosidase were both found to be 50°C. Similarly, the optimum reaction pH was 7.5 for both the free and the entrapped enzyme. The immobilized β‐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 × 10 −5 min −1 . © 1999 John Wiley & Sons, Inc. J Appl Polym Sci 72: 1367–1373, 1999