PH-induced interface protein structure changes to adjust the stability of tilapia protein isolate emulsion prepared by high-pressure homogenization.

ABSTRACT: The pH is a crucial external factor affecting the structure and emulsification characteristics of proteins. The current study aimed to reveal the correlation between the secondary structure changes and tilapia protein isolate (TPI) emulsion stability under different pH (3.0-10.0) prepared by high-pressure homogenization. The results showed that TPI with significantly increased solubility and emulsifying properties when the pH keep away from the isoelectric point (pH 5.0). Meanwhile, TPI emulsions presented significantly enhanced stability (with decreased particle size, increased zeta potential, creaming index close to 0, and uniform dispersion of droplets) at pH 3.0 and 10.0. Interface-adsorbed protein mainly consists of a myosin-heavy chain and actin, and the secondary structure was signi

SUBMITTER: Liu Q 

PROVIDER: S-EPMC11456911 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature