Pulsed electric field enhances glucose glycation and emulsifying properties of bovine serum albumin: Focus on polarization and ionization effects at a high reaction temperature

Int J Biol Macromol. 2024 Feb;257(Pt 1):128509. doi: 10.1016/j.ijbiomac.2023.128509. Epub 2023 Dec 3.

Abstract

Previous studies demonstrated that the non-thermal effects of pulsed electric fields can promote protein glycation below 40 °C, but it does not always enhance the emulsifying properties of proteins, such as in the bovine serum albumin/glucose model. Therefore, the aim of this study was to investigate the impact of non-thermal effects on the glucose glycation and emulsification properties of bovine serum albumin at 90 °C. The results of circular dichroism, surface hydrophobicity, and molecular dynamics simulations showed that the polarization effect increased the degree of glycation of bovine serum albumin-glucose conjugates from 12.82 % to 21.10 % by unfolding protein molecule, while the emulsifying stability index was increased from 79.17 to 100.73 compared with the control. Furthermore, the results of principal component analysis and Pearson correlation analysis indicated that the ionization effect and the free radicals generated by pulsed electric fields significantly (p < 0.05) inhibited browning and reduced free sulfhydryl content. This study demonstrated that pulsed electric fields combined with heating can prepare glycated proteins with good emulsifying properties in a short period of time and at temperatures lower than conventional heating while reducing energy consumption. This processing strategy has potential applications in improving the emulsifying performance of highly stable proteins.

Keywords: Bovine serum albumin; Emulsion stability; Maillard reaction; Non-thermal reactions; Pulsed electric field.

MeSH terms

  • Glucose
  • Hydrophobic and Hydrophilic Interactions
  • Maillard Reaction*
  • Serum Albumin, Bovine*
  • Temperature

Substances

  • Serum Albumin, Bovine
  • Glucose