Enhancing biocatalyst performance through immobilization of lipase (Eversa® Transform 2.0) on hybrid amine-epoxy core-shell magnetic nanoparticles

Int J Biol Macromol. 2024 Apr;264(Pt 2):130730. doi: 10.1016/j.ijbiomac.2024.130730. Epub 2024 Mar 10.

Abstract

Magnetic nanoparticles were functionalized with polyethylenimine (PEI) and activated with epoxy. This support was used to immobilize Lipase (Eversa® Transform 2.0) (EVS), optimization using the Taguchi method. XRF, SEM, TEM, XRD, FTIR, TGA, and VSM performed the characterizations. The optimal conditions were immobilization yield (I.Y.) of 95.04 ± 0.79 %, time of 15 h, ionic load of 95 mM, protein load of 5 mg/g, and temperature of 25 °C. The maximum loading capacity was 25 mg/g, and its stability in 60 days of storage showed a negligible loss of only 9.53 % of its activity. The biocatalyst demonstrated better stability at varying temperatures than free EVS, maintaining 28 % of its activity at 70 °C. It was feasible to esterify free fatty acids (FFA) from babassu oil with the best reaction of 97.91 % and ten cycles having an efficiency above 50 %. The esterification of produced biolubricant was confirmed by NMR, and it displayed kinematic viscosity and density of 6.052 mm2/s and 0.832 g/cm3, respectively, at 40 °C. The in-silico study showed a binding affinity of -5.8 kcal/mol between EVS and oleic acid, suggesting a stable substrate-lipase combination suitable for esterification.

Keywords: Babassu oil; Biofuels; Eversa lipase; Heterofunctional immobilization.

MeSH terms

  • Enzyme Stability
  • Enzymes, Immobilized / chemistry
  • Esterification
  • Lipase* / chemistry
  • Magnetite Nanoparticles*
  • Plant Oils / chemistry

Substances

  • Lipase
  • Enzymes, Immobilized
  • Magnetite Nanoparticles
  • Plant Oils