On the Emulsifying Properties of Self-Assembled Pea Protein Particles.
Journal
Langmuir : the ACS journal of surfaces and colloids
ISSN: 1520-5827
Titre abrégé: Langmuir
Pays: United States
ID NLM: 9882736
Informations de publication
Date de publication:
20 10 2020
20 10 2020
Historique:
pubmed:
30
9
2020
medline:
22
6
2021
entrez:
29
9
2020
Statut:
ppublish
Résumé
Pea proteins are promising oil-in-water emulsifying agents at both neutral and acidic conditions. In an acidic environment, pea proteins associate to form submicrometer-sized particles. Previous studies suggested that the emulsions at acidic pH were stabilized due to a Pickering mechanism. However, protein particles can be in equilibrium with protein molecules, which could play a significant role in the stabilization of emulsion droplets. Therefore, we revisited the emulsion stabilization mechanism of pea proteins at pH 3 and investigated whether the protein particles or the protein molecules are the major emulsifying agent. The theoretical and experimental surface load of dispersed oil droplets were compared, and we found that protein particles can cover only 3.2% of the total oil droplet surface, which is not enough to stabilize the droplets, whereas protein molecules can cover 47% of the total oil droplet surface. Moreover, through removing protein particles from the mixture and emulsifying with only protein molecules, the contributions of pea protein molecules to the emulsifying properties of pea proteins at pH 3 were evaluated. The results proved that the protein molecules were the primary stabilizers of the oil droplets at pH 3.
Identifiants
pubmed: 32988196
doi: 10.1021/acs.langmuir.0c01955
pmc: PMC7586397
doi:
Substances chimiques
Emulsifying Agents
0
Emulsions
0
Pea Proteins
0
Water
059QF0KO0R
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
12221-12229Références
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