Comparison of the immobilization of lipase from Pseudomonas fluorescens on divinylsulfone or p-benzoquinone activated support

Int J Biol Macromol. 2019 Aug 1:134:936-945. doi: 10.1016/j.ijbiomac.2019.05.106. Epub 2019 May 20.

Abstract

NiZnFe2O4 superparamagnetic nanoparticles were coated with silica by impregnation with tetraethoxysilane (TEOS) and further activated with divinylsulfone (DVS) and p-benzoquinone (BQ) for covalent immobilization lipase from Pseudomonas fluorescens (PFL), producing the biocatalysts TEOS-NANO-DVS-PFL and TEOS-NANO-BQ-PFL. The optimal conditions for enzyme immobilization were found to be pH 7 and 0.1 M of both activating reagents. PFL was also immobilized on TEOS nanoparticles without any activation as a reference (TEOS-NANO-PFL). Results indicated that TEOS could be released from the nanoparticles at alkaline pH value. Optimal TEOS-NANO-PFL exhibited a recovered activity of 55% and a t1/2(60°C) of just over 150 min; while TEOS-NANO-DVS-PFL showed 82% of activity recovered and t1/2(60°C) of 225 min; being the TEOS-NANO-BQ-PFL the biocatalyst offering the best results (89% of recovered activity and a half-life over 1440 min), the maximum enzyme load was ≈300 U/g.

Keywords: Adsorption; Covalent binding; Enzyme immobilization; Enzyme stabilization; Lipase.

MeSH terms

  • Benzoquinones / chemistry*
  • Enzyme Stability
  • Enzymes, Immobilized*
  • Hydrogen-Ion Concentration
  • Lipase / chemistry*
  • Metal Nanoparticles / chemistry
  • Models, Molecular
  • Protein Conformation
  • Pseudomonas fluorescens / enzymology*
  • Spectroscopy, Fourier Transform Infrared
  • Sulfones / chemistry*
  • Thermodynamics

Substances

  • Benzoquinones
  • Enzymes, Immobilized
  • Sulfones
  • Lipase