Functionality Enhancement of Pea Protein Powder via High-Intensity Ultrasound: Screening in-vitro Digestion, o/w Emulsion Properties and Testing in Gluten-Free Bread.

Abstract

Structural modification of protein prior to food application is an emergent approach to improve functionalization. The effectiveness of high-power ultrasound at varying amplitudes (0-100%) on the properties of pea protein powder was investigated in this study. The resulting modification was also tested with model gluten-free bread formulation and by screening the emulsion properties within vegetable oil. The 50% and beyond amplitude levels had significant impact on protein solubility, viscosity, Fourier Transform Infrared (FTIR) spectra, emulsion activity and stability. Foaming capacity and stability were enhanced with 75 and 100% amplitudes while the 25% amplitude exhibited the highest absolute zeta-potential. There was a concomitant increase in ultrasound amplitude and oil-binding capacity (2.83-6.43g/g) where the water-holding capacity gradually decreased (5.78-3.61g/g) with the increase in ultrasound power. The increase in ultrasound power led to decrease in L* values but progressively increased the total color difference (ΔE). Sonication (50% amplitude) also promoted the in-vitro digestibility of proteins by 22% as compared to the untreated sample. Scanning electron microscopy (SEM) fairly depictured the structural modification and FTIR spectra clearly demonstrated conformational changes in protein powders. The fortification with restructured pea protein powder significantly affected the volume and adhesiveness of glutenfree bread.