Enhancing the Usability of Pea Protein Isolate in Food Applications through Modifying Its Structural and Sensory Properties via Deamidation by Glutaminase

摘要: This study aimed to demonstrate the feasibility of improving properties pea protein isolate (PPI) related food applications via deamidation with glutaminase. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared (FT-IR) profiling revealed that current glutaminase treatment did not change basic subunit composition. However, it allowed a certain extent unfolding conformational reorganization generate more flexible extended proteins reduced average particle size hydrophobic groups exposed. The underlying mechanisms might include reduction β-sheets antiparallel increase β-turn structure. Moreover, time was importance. A 12 h generally better than 24 treatment, PPI treated at 50 °C for degree 56.1% exhibited significantly improved solubility, homogeneity, dispersibility, suspendability beany flavor, grittiness, lumpiness (compared those untreated PPI). Thus, offers promising approach enhancing usability applicability proteins.