Characterization of the activity of β-galactosidase immobilized on Teflon membranes preactivated with different monomers by γ-irradiation

✍ Scribed by M. S. Mohy Eldin; U. Bencivenga; M. Portaccio; S. Stellato; S. Rossi; M. Santucci; P. Canciglia; D. Castagnolo; F. S. Gaeta; D. G. Mita

• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 318 KB
• Volume: 68
• Category: Article
• ISSN: 0021-8995
• DOI: 10.1002/(sici)1097-4628(19980425)68:4<613::aid-app13>3.0.co;2-s

✦ Synopsis

The activity of b-galactosidase, immobilized by grafting technique on Teflon membranes preactivated with four different monomers, has been characterized from the biochemical and biophysical points of view. The monomers used were acrylic acid or acrylamide, or methacrylic acid and 2-hydroxyethyl methacrylate. When 2-hydroxyethyl methacrylate was used in the second grafting, the first three monomers have been used in the first modification step. The behavior of the free and immobilized enzyme has been analyzed as a function of temperature and pH. For each catalytic membrane, we have found general equations relating the absolute enzyme activity to pH and temperature. From these expressions, the experimental conditions giving the best yield of each catalytic membrane have been calculated. The kinetic parameters for the four membranes have also been determined. The advantages of using these membranes in nonisothermal bioreactors are also indicated.