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
Structure and activity of trypsin in reverse micelles
โ Scribed by Peter WALDE; Qiaoqian PENG; Nitin W. FADNAVIS; Ezio BATTISTEL; Pier Luigi LUISI
- Book ID
- 115125733
- Publisher
- John Wiley and Sons
- Year
- 1988
- Tongue
- English
- Weight
- 1007 KB
- Volume
- 173
- Category
- Article
- ISSN
- 1432-1327
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๐ SIMILAR VOLUMES
Trypsin inhibitor was converted to hydrophobic states by covalently combining cholesteryl groups using an acylation reaction, and was immobilized in reverse micelles composed of a nonionic surfactant. Using this reverse micellar phase containing trypsin inhibitor as an affinity ligand, trypsin was s
This paper presents some new results concerning the evolution of the local order in the mineral core of reverse micelles during their synthesis. It is shown that no drastic structural change occurs during the reaction, the mineral core remaining amorphous with a local order close to calcite one.