Purification and improvement of the functional properties of Rhizopus oryzae lipase using immobilization techniques

- 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).