Effect Of Grinding On The Structure Of Pea Protein Isolate And The Rheological Properties Of Its Acid-Induced Gels

The purpose of this study was to expand the application range of pea protein isolates by improving the rheological properties of their acid-induced gels. A pea protein isolate was ground for different durations, and changes in the structure and properties of its gels were studied. Furthermore, the influence mechanism of grinding on gelation was revealed. The results showed that grinding slightly changed the secondary structure of the pea protein isolate and had a great impact on its tertiary structure. Compared with the unground pea protein isolate, the solubility of the ground pea protein isolate increased from 45.89% to 69.84%, and the water-holding capacity of the gels increased from 52.04% to 94.67% at 7.5 min of grinding. After grinding for 15 min, the particle size of the pea protein isolate decreased from 1292.4 to 945.7 nm, and the polydispersity index decreased from 0.387 to 0.321. Rheological measurements showed that the storage modulus (G '), viscosity and recovery of protein gel samples improved after grinding. Thus, grinding enhanced the potential of protein gels for new applications.