Effects of Ultrasound-Transglutaminase Treatment on the Properties of Pea Protein Isolate Gel
摘要
Pea protein isolate (PPI) was treated by ultrasound (US) and then subjected to transglutaminase (TGase)-catalyzed cross-linking to prepare PPI gels. Ultrasonic pretreatment effectively improved gel hardness, springiness, and chewiness by reducing particle size and enhancing protein dispersion. Subsequent TGase treatment further reinforced the gel matrix through covalent crosslinking, resulting in a more robust three-dimensional network structure. The effect of US-TGase treatment demonstrated substantial improvements in water holding capacity (WHC) and thermal stability of the PPI gels. Microstructural analysis revealed that ultrasonic treatment generated a more compact gel network with reduced pore size, which was subsequently stabilized by TGase-induced covalent bonding. These findings suggest that the combined application of ultrasonic pretreatment and enzymatic cross-linking represents an effective strategy for optimizing the functional properties and structural integrity of PPI-based gels.
Graphical Abstract