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

Tipo de material: TextoTextoSeries ; Journal of Molecular Catalysis B: Enzymatic, 57(1-4), p.171-176, 2009Trabajos contenidos:
  • Cabrera, Z
  • Fernandez-Lorente, G
  • Fernandez-Lafuente, G
  • Palomo, J.M
  • Guisan, J.M
Tema(s): Recursos en línea: Resumen: 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
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Item type Current library Collection Call number Status Date due Barcode
Documentos solicitados Documentos solicitados CICY Documento préstamo interbibliotecario Ref1 B-11695 (Browse shelf(Opens below)) Available

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

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