Gel entrapped enzymes: Kinetic studies of immobilized β-galactosidase
✍ Scribed by I. Hinberg; R. Korus; K. F. O'Driscoll
- Publisher
- John Wiley and Sons
- Year
- 1974
- Tongue
- English
- Weight
- 876 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0006-3592
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Trypsin and a-chymotrypsin were immobilized by gel entrapment in polyacrylamide cross-linked with N , Nmethylenebisacrylamide. The immobilized enzymes are catalytically efficient in suspensions of reverse micelles formed i n isooctane by bis(2-ethylhexyl) sodium sulfosuccinate) (AOT) and water. Both
b-Galactosidase was immobilized in/on poly(2-hydroxyethyl methacrylate) (pHEMA) membranes by two di †erent methods : adsorption on Cibacron F3GA derivatized pHEMA membranes (pHEMA-CB), and entrapment in the bulk of the pHEMA membranes. The maximum b-galactosidase adsorption on pHEMA-CB membranes was