Controlled ethanol-mediated polyphenol removal from sunflower meal: Impact on physicochemical, structural,...

Polyphenols present in sunflower meal act on sunflower proteins by reacting directly with their structures and thus influencing their purity, solubility, crystallinity, and functionality. However, the effect on these properties of varying concentrations of ethanol used in dephenolization has yet to be explored. The present study aimed to explore the impact of dephenolization using varying ethanol concentrations (60%, 70%, 80%, and 90%) on the physicochemical, color, thermal, structural, functional, and flow behavior of protein isolates extracted from sunflower meal.

Protein isolates originating from meals that were dephenolized using higher ethanol concentrations exhibited a protein content of 836.10 g kg^-1. As the concentration of ethanol increased, a reduction in crystallinity was observed from 24% to 14.15%. Fourier transform infrared (FTIR) spectroscopy revealed marked shifts in major peaks within the 1600 to 1700 cm-1 wavelength range, indicating significant structural and conformational changes. Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) results demonstrated that dephenolization caused decline in molecular weight ranging from 25 kDa to 60 kDa. Dephenolization induced significant changes in surface morphology resulting in more heterogeneous and disordered surfaces as indicated by field emission-scanning electron microscopy (FE-SEM) micrographs. Overall improvement in the functional properties was observed, with an increase in solubility from 15.20% to 22.03%. Improvement in the flow behavior with an increase in porosity from 38% to 60% was also observed, due to dephenolization.

Dephenolization using 90% ethanol induced structural changes that enhanced physicochemical and functional characteristics of sunflower protein isolates by improving purity and solubility, reducing crystallinity, and increasing flow behavior. © 2024 Society of Chemical Industry.