Candida rugosa lipase immobilization on hydrophilic charged gold nanoparticles as promising biocatalysts: Activity and stability investigations

Colloids Surf B Biointerfaces. 2015 Jul 1:131:93-101. doi: 10.1016/j.colsurfb.2015.04.046. Epub 2015 Apr 27.

Abstract

In this work, a simple and versatile methodology to obtain two different bioconjugated systems has been developed by the immobilization of Candida rugosa lipase (CRL) on hydrophilic gold nanoparticles functionalized with 2-diethylaminoethanethiol hydrochloride (DEA) or with sodium 3-mercapto-1-propanesulfonate (3MPS), namely Au-DEA@CRL and Au-3MPS@CRL. Both spectroscopic and morphological properties of metal nanoparticles have been deeply investigated. The enzyme loading and lipolytic activity of AuNPs@CRL bioconjugates have been studied with respect to different surface functionalization and compared with the free enzyme. Some physical and chemical parameters had a strong effect on enzyme activity and stability, that were improved in the case of the Au-DEA@CRL bioconjugate, which showed a remarkable biocatalytic performance (95% of residual lipolytic activity compared with free CRL) and stability in experimental conditions concerning pH (range 5-8) and temperature (range 20-60°C), as often required for the industrial scale up of catalytic systems.

Keywords: Biocatalysis; Candida rugosa lipase; Gold nanoparticles; Lipase immobilization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocatalysis
  • Candida / enzymology*
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry
  • Enzymes, Immobilized / metabolism
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism*
  • Gold / chemistry*
  • Hydrogen-Ion Concentration
  • Hydrophobic and Hydrophilic Interactions
  • Lipase / chemistry
  • Lipase / metabolism*
  • Lipolysis
  • Metal Nanoparticles / chemistry*
  • Metal Nanoparticles / ultrastructure
  • Microscopy, Atomic Force
  • Microscopy, Electron, Scanning
  • Microscopy, Electron, Transmission
  • Molecular Structure
  • Sulfhydryl Compounds / chemistry
  • Temperature

Substances

  • 3-mercapto-1-propanesulfonate
  • Enzymes, Immobilized
  • Fungal Proteins
  • Sulfhydryl Compounds
  • Gold
  • Lipase