Elucidation of the structure, antioxidant, and interfacial properties of flaxseed proteins tailored by microwave treatment

Abstract

The microwave treatment is commonly applied to flaxseed to release nutrients, inactivate enzymes, remove cyanogens, and intensify flavors. The current study aimed to explore the influences of microwave exposure on the antioxidant and interfacial properties of flaxseed protein isolates (FPI), focusing on the altering composition and molecular structure. The results showed that after microwave exposure (700 W, 1–5 min), more compact assembly of storage proteins and subsequent permeation by membrane fragments of oil bodies occurred for cold-pressing flaxseed flours. Moreover, the particle sizes of FPI was progressively reduced with the decrement ranged from 37.84 to 60.66% (P<0.05), whereas the zeta potential values initially decreased and then substantially recovered during 1–5 min of microwave exposure. The conformation unfolding, chain cross-linking, and depolymerization were sequentially induced for FPI based on the analysis of fluorescence emission spectra, secondary structure, and protein subunit profiles, thereby affecting the dispersion or aggregation properties between albumin and globulin fractions in FPI. Microwave exposure retained specific phenolic acids and superior in vitro antioxidant activities of FPI. The inferior gas–water interface absorption and the loose/porous assembly structure were observed for the foams prepared by FPI, concurrent with obviously shrinking foaming properties upon microwave exposure. Improving oil–water interface activities of FPI produced the emulsion droplets with descending sizes and dense interface coating, which were then mildly destabilized due to the lipid leakage and weakened rheological behavior with microwave exposure extended to 5 min. Our findings elucidated that microwave treatment could tailor the application functionality of protein fractions in flaxseed based on their in situ structural remodeling.