Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols

Molecules. 2020 Jan 15;25(2):350. doi: 10.3390/molecules25020350.

Abstract

Lipase B from Candida antarctica immobilized by covalent binding on sebacoyl-activated chitosan-coated magnetic nanoparticles proved to be an efficient biocatalyst (49.2-50% conversion in 3-16 h and >96% enantiomeric excess) for the enzymatic kinetic resolution of some racemic heteroarylethanols through transesterification with vinyl acetate. Under optimal conditions (vinyl acetate, n-hexane, 45 °C), the biocatalyst remains active after 10 cycles.

Keywords: chitosan; covalent immobilization; enzymatic kinetic resolution; lipase B from Candida antarctica; magnetic nanoparticle.

MeSH terms

  • Candida / enzymology*
  • Catalysis
  • Chitosan / chemistry*
  • Enzymes, Immobilized / chemistry
  • Enzymes, Immobilized / metabolism*
  • Esterification
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism*
  • Kinetics
  • Lipase / chemistry
  • Lipase / metabolism*
  • Magnetite Nanoparticles / chemistry*
  • Stereoisomerism
  • Vinyl Compounds / chemistry*

Substances

  • Enzymes, Immobilized
  • Fungal Proteins
  • Magnetite Nanoparticles
  • Vinyl Compounds
  • Chitosan
  • Lipase
  • lipase B, Candida antarctica
  • vinyl acetate