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 meth
✦ LIBER ✦
Covalent immobilization of β-galactosidase on carrageenan coated with chitosan
✍ Scribed by Magdy M.M. Elnashar; Mohamed A. Yassin
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 425 KB
- Volume
- 114
- Category
- Article
- ISSN
- 0021-8995
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The dependence of grafting and catalytic activity on the pore size of nylon membranes grafted with different DGDA concentrations and loaded with -galactosidase is discussed. Membrane pore sizes were 0.2, 1.2, and 3.0 m. Grafting and enzyme activity, all other experimental conditions being the same,