Improving lipase activity by immobilization and post-immobilization strategies

Jose M. Palomo, Marco Filice, OSCAR ENRIQUE ROMERO ORMAZABAL, Jose M. Guisan

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

11 Scopus citations

Abstract

One important parameter for the application of lipase catalysts in chemical industries is the specific activity displayed towards natural or unnatural substrates. Different strategies to enhance the lipase activity have been described. The immobilization of lipases on hydrophobic supports by interfacial adsorption at low ionic strength permitted the hyper-activation of these enzymes by fixing the open conformation of the lipase on the hydrophobic support. Improvements of activity from 1.2- up to 20-fold with respect to the initial one have been observed for lipases from different sources. A second strategy was based on the presence of additives, in particular surfactants or ionic liquids, with hydrophobic character to enhance the activity of lipases immobilized on macroporous supports up to eightfold and even more than 100-fold in some cases for soluble lipases. Finally, a third strategy to improve the activity in immobilized lipases was based on a site-directed chemical modification of the protein by glycosylation on the enzyme N-terminal group or on a unique reactive cysteine of the enzyme by disulfide exchange using different tailor-made disulfide activated activated polymers.

Original languageEnglish
Title of host publicationImmobilization of Enzymes and Cells
Subtitle of host publicationThird Edition
PublisherHumana Press Inc.
Pages255-273
Number of pages19
ISBN (Print)9781627035491
DOIs
StatePublished - 1 Jan 2013

Publication series

NameMethods in Molecular Biology
Volume1051
ISSN (Print)1064-3745

Keywords

  • Activation
  • Additives
  • Immobilization
  • Lipase
  • Polymers
  • Site-directed modification

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