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

Authors

M. Arica, T. Baran, A. Deni̇zli̇

Published

1999

DOI

10.1002/(SICI)1097-4628(19990606)72:10<1367::AID-APP17>3.0.CO;2-D

Citations

19

Abstract

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 Km 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 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 (kiop) 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

Cite this article

BibTeX

@article{m1999,
  title   = {β‐Galactosidase immobilization into poly(hydroxyethyl methacrylate) membrane and performance in a continuous system},
  author  = {M. Arica and T. Baran and A. Deni̇zli̇},
  doi     = {10.1002/(SICI)1097-4628(19990606)72:10<1367::AID-APP17>3.0.CO;2-D},
  year    = {1999}
}

← All publications DOI: 10.1002/(SICI)1097-4628(19990606)72:10<1367::AID-APP17>3.0.CO;2-D