Development of a magnetically stabilized fluidized bed bioreactor for enzymatic synthesis of 2-ethylhexyl oleate

Bioprocess Biosyst Eng. 2023 Nov;46(11):1665-1676. doi: 10.1007/s00449-023-02928-8. Epub 2023 Oct 10.

Abstract

This study aimed to develop and investigate the synthesis of 2-ethylhexyl oleate catalyzed by Candida antarctica lipase immobilized on magnetic poly(styrene-co-divinylbenzene) (STY-DVB-M) particles in a magnetically stabilized fluidized bed reactor (MSFBR) operated in continuous mode. The physical properties of the copolymer were characterized by Fourier-transform infrared spectroscopy (FTIR), differential scanning calorimetry (DSC), and thermogravimetric analysis (TGA). The glass transition temperature was 85.68 °C, and the onset of thermal degradation occurred at 406.66 °C. Syntheses were performed at 50 °C using a space time of 12 h and a bed porosity of 0.892. Assays were conducted to assess the influence of magnetic field intensity (5 to 15 mT) on reaction yield, ester concentration, and productivity. The highest productivity was 0.850 ± 0.023 mmol g-1 h-1, obtained with a magnetic field intensity of 15 mT. An operational stability test was performed under these conditions, revealing a biocatalyst half-life of 2148 h (179 operation cycles) and a thermal deactivation constant of 3.23 × 10-4 h-1 (R2 = 0.9446). Computational simulations and mathematical modeling were performed using Scilab based on ping-pong bi-bi kinetics and molar balances of reaction species. The model provided consistent results of interstitial velocity and good prediction of reaction yields, with R2 = 0.926. These findings demonstrate that the studied technique can provide improvements in biocatalytic processes, representing a promising strategy for the enzymatic synthesis of 2-ethylhexyl oleate.

Keywords: Computer simulation; Esterification; Immobilized lipase; Magnetic polymer support; Magnetically stabilized fluidized bed bioreactor.

MeSH terms

  • Biocatalysis
  • Bioreactors
  • Enzymes, Immobilized* / chemistry
  • Esterification
  • Lipase / chemistry
  • Oleic Acid*

Substances

  • Oleic Acid
  • Enzymes, Immobilized
  • Lipase