Immobilization of Candida rugosa lipase onto an eco-friendly support in the presence of ionic liquid

Bioprocess Biosyst Eng. 2015 May;38(5):805-14. doi: 10.1007/s00449-014-1322-2. Epub 2014 Nov 13.

Abstract

Candida rugosa lipase (CRL) was immobilized on an eco-friendly support poly(3-hydroxybutyrate-co-hydroxyvalerate) (PHBV), by physical adsorption, using different ionic liquids (ILs) as immobilization additives. This was to investigate the influence of cationic core ([C4mpy]Cl, [C4min]Cl), of anions ([C4min]Cl, [C4min]N(CN)2, [C4min]Tf2N), and of cation chain length ([C2min]Tf2N, [C4min]Tf2N) in the immobilization process. The immobilized biocatalysts (IB) were characterized with respect to the morphological, physico-chemical properties, total activity recovery yield (Ya), and biochemical properties of more efficient IB were evaluated. Initially, it was found that the change of cationic core did not influence in Ya compared to the control. With change of anions, it was seen that the best result was obtained for the more hydrophobic anion (Tf2N), and finally increasing the cation chain length increased Ya. IB most efficient with [C4min]Tf2N obtained 78 % of Ya, more than twice the control value (30 %) and a considerable enhancement of operational stability compared with the control.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Anions
  • Candida / enzymology*
  • Catalysis
  • Cations
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry*
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Industrial Microbiology*
  • Ionic Liquids / chemistry*
  • Ions
  • Lipase / chemistry*
  • Microscopy, Electron, Scanning
  • Porosity
  • Spectroscopy, Fourier Transform Infrared

Substances

  • Anions
  • Cations
  • Enzymes, Immobilized
  • Ionic Liquids
  • Ions
  • Lipase