β-Galactosidase immobilization into poly(hydroxyethyl methacrylate) membrane and performance in a continuous system

✍ Scribed by M. Yakup Arica; Türker Baran; Adil Denizli

• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 211 KB
• Volume: 72
• Category: Article
• ISSN: 0021-8995
• DOI: 10.1002/(sici)1097-4628(19990606)72:10<1367::aid-app17>3.0.co;2-d

✦ Synopsis

The activity of ␤-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 ␤-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 ␤-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 ϫ 10 Ϫ5 min Ϫ1 .