Role of the pea protein aggregation state on their interfacial properties
Katherine Findlay Grasberger, Frederik W. Lund, Adam Cohen Simonsen, Marianne Hammershøj, Peter Fischer, Milena Corredig
Journal of Colloid and Interface Science
Abstract
Atomic force microscopy provided evidence of interfaces packed with protein oligomers regardless of the treatment. Differences in adsorption kinetics and interfacial shear rheology depending on oil polarity suggested different interfacial structures. A polydisperse mixture of protein oligomers resulted in increased rearrangements and protein-protein interactions at the interface. Homogenization of commercial proteins resulted in a lower interfacial tension and less elastic interfaces compared to those of native proteins due to the presence of larger aggregates. This study highlights how the interfacial properties can be related to the protein aggregation state resulting from differences in processing history.
Extracted Claims
2 claims extracted from this paper into the knowledge graph
homogenization results in lower interfacial tension and less elastic interfaces
“Homogenization of commercial proteins resulted in a lower interfacial tension and less elastic interfaces compared to those of native proteins due to the presence of larger aggregates”
polydisperse mixture of protein oligomers results in increased rearrangements and protein-protein interactions at the interface
“A polydisperse mixture of protein oligomers resulted in increased rearrangements and protein-protein interactions at the interface”