TY  - BOOK
AU  - Cabrera,Z.
AU  - Fernandez-Lorente,G.
AU  - Fernandez-Lafuente,G.
AU  - Palomo,J.M.
AU  - Guisan,J.M.
TI  - Novozym 435 displays very different selectivity compared to lipase from Candida antarctica B adsorbed on other hydrophobic supports
KW  - LEWATIT
KW  - INTERFACIAL ACTIVATION OF LIPASES
KW  - ENANTIOSELECTIVITY
KW  - HYDROPHOBIC SUPPORTS
KW  - MODULATION OF ENZYME PROPERTIES
KW  - MANDELIC ACID
KW  - 3-PHENYLGLUTARIC ACID DIMETHYL DIESTER
N2  - This paper shows that the properties of lipase B fromCandida antarctica (CAL-B)may be easily modulated using different hydrophobic supports to immobilize it (octyl and butyl-agarose, octadecyl-Sepabeads or Lewatit). CAL-B could be fully desorbed from the supports by just incubating the biocatalyst with Triton X-100, although the concentration of detergent necessary was to fully desorb the enzyme varied with the support employed (from 1
UR  - https://drive.google.com/file/d/1uX-tB3k0FC8srmULNl_NHLDpcxeJYlgy/view?usp=drivesdk
ER  -