Role of the pea protein aggregation state on their interfacial properties
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Date
2024-03-15
Publication Type
Journal Article
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yes
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Abstract
Hypothesis: Plant protein ingredients from similar sources can vary in functionality not only because of compositional differences, but also because of differences in their structure depending on their processing history. It is essential to understand these distinctions to develop novel food emulsion using plant proteins. It is hypothesized that differing interfacial properties can be attributed to their structures, aggregation, and colloidal states. Experiments: The adsorption behavior of a commercial protein isolate, homogenized or non-homogenized, was compared to a mildly extracted isolate to evaluate the effect of aggregation state and structural differences. After characterization of the particle size and protein composition, the interfacial properties were compared. Findings: 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.
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published
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Journal / series
Volume
658
Pages / Article No.
156 - 166
Publisher
Elsevier
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Edition / version
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Date collected
Date created
Subject
Plant proteins; Pea protein; Colloidal state; Interfacial behavior; Food emulsions; Oil-water interface
Organisational unit
08821 - Fischer, Peter (Tit.-Prof.)
Notes
Funding
212079 - Green proteins: Do we have to rethink food emulsion? (SNF)