Impact of dynamic high-pressure microfluidization on conformation and gel properties of peanut protein isolates

• Published in: Journal of food engineering Vol. 392; p. 112495
• Main Authors: Li, Suhong, Liu, Yu, Liu, Chenfei, Wang, Chunyan
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.05.2025
• Subjects: Conformation; disulfide bonds; disulfides; Dynamic high-pressure microfluidization; Gel property; gels; hardness; hydrophobicity; microstructure; peanut protein; Peanut protein isolate; protein isolates; water holding capacity; Peanut protein isolate; Gel property; Dynamic high-pressure microfluidization; Conformation
• ISSN: 0260-8774
• DOI: 10.1016/j.jfoodeng.2025.112495

The impact of dynamic high-pressure microfluidization (DHPM) (30–150 MPa) on the structure of peanut protein isolate (PPI) and PPI gel behavior and microstructural properties were studied. The research found that DHPM treatment significantly decreased the volume-mean diameter of PPI (p < 0.05), and induced the β-sheets, β-turn and random coils to transform into α-helix structures. With increased pressure, the hydrophobic groups of PPI were exposed to the outside, thus the surface hydrophobicity of PPI enhanced, and the sulfhydryl content and disulfide bond content increased significantly (p < 0.05) compared to control samples. Furthermore, the hardness of MTGase-induced gel increased gradually from 0.14 N (0.1 MPa) to 0.35 N (150 MPa). And the water-holding capacity of PPI gel reached its maximum at 90 MPa. The types of intermolecular interactions in the PPI gel were mainly hydrophobic interactions and disulfide bonds. Gʹ and Gʹʹ increased significantly from 30 MPa to 90 MPa. The microstructure of the gel systems upon 90 MPa and 120 MPa treatment showed more optimal surface appearance. These results indicate that the DHPM treatment could provide a new way to enhance the gel properties of PPI. •The impact of DHPM on conformation of PPI and gel properties were analyzed.•DHPM affected protein aggregation, change PPI tertiary and quaternary structure.•The partially unfolding of PPI promoted protein-protein interactions.•PPI gel property was improved and the ordered and compact gel formed.•DHPM would be an effective tool for expanding the application of PPI in food.