| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6531120 | Journal of Molecular Catalysis B: Enzymatic | 2014 | 6 Pages |
Abstract
- Rhizopus oryzae lipase (ROL) was fully purified by selective adsorption on hydrophobic supports (phenyl-Toyopearl).
- ROL was hyperactivated (up to a 250%) by adsorption on highly hydrophobic supports (octyl-Separose and C18-Sepabeads).
- Multipoint covalent attachment of ROL on highly activated glyoxyl agarose improves thermal stability 300-fold regarding to soluble enzyme and CNBr-Sepharose derivative.
- Enantioselectivity strongly varies with different ROL derivatives (e.g., from 3.5 for CNBr-Sepharose derivative to 22 for C18-Sepabeads derivative).
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
N. Ghattas, M. Filice, F. Abidi, J.M. Guisan, A. Ben Salah,