Functionalizing walnut protein via consecutive purification and ultrasound modification: Self-assembled structure and interfacial properties.

ABSTRACT: The preparation of plant proteins generally involves three independent steps, which is time-consuming. Here, we integrated these three steps into one consecutive process (one-step preparation), which involved alkali extraction, membrane purification, and ultrasound modification. The obtained walnut protein was evaluated in terms of self-assembled structure, interfacial behaviors, and emulsifying properties. Compared with the traditional preparation method, our one-step preparation regulated the aggregation of walnut protein from a dissolved state to a well-organized assembly. When the ultrasound modification was conducted at 10 W/mL for 30 min, the walnut protein (WP-U2) showed the highest surface hydrophobicity (H₀ = 36704), the smallest particle size (205 nm), and highest solu

SUBMITTER: Zhou J 

PROVIDER: S-EPMC12348030 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature