Novozym 435 displays very different selectivity compared to lipase from Candida antarctica B adsorbed on other hydrophobic supports 

 -  Journal of Molecular Catalysis B: Enzymatic, 57(1-4), p.171-176, 2009 .
<br/><br/> 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 
<br/><br/><label>Subjects--Topical Terms: </label><br/>LEWATIT<br/>INTERFACIAL ACTIVATION OF LIPASES<br/>ENANTIOSELECTIVITY<br/>HYDROPHOBIC SUPPORTS<br/>MODULATION OF ENZYME PROPERTIES<br/>MANDELIC ACID<br/>3-PHENYLGLUTARIC ACID DIMETHYL DIESTER