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On the Emulsifying Properties of Self-Assembled Pea Protein Particles

[Image: see text] 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 me...

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Autores principales: Sridharan, Simha, Meinders, Marcel B. J., Bitter, Johannes H., Nikiforidis, Constantinos V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7586397/
https://www.ncbi.nlm.nih.gov/pubmed/32988196
http://dx.doi.org/10.1021/acs.langmuir.0c01955
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author Sridharan, Simha
Meinders, Marcel B. J.
Bitter, Johannes H.
Nikiforidis, Constantinos V.
author_facet Sridharan, Simha
Meinders, Marcel B. J.
Bitter, Johannes H.
Nikiforidis, Constantinos V.
author_sort Sridharan, Simha
collection PubMed
description [Image: see text] 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.
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spelling pubmed-75863972020-10-27 On the Emulsifying Properties of Self-Assembled Pea Protein Particles Sridharan, Simha Meinders, Marcel B. J. Bitter, Johannes H. Nikiforidis, Constantinos V. Langmuir [Image: see text] 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. American Chemical Society 2020-09-28 2020-10-20 /pmc/articles/PMC7586397/ /pubmed/32988196 http://dx.doi.org/10.1021/acs.langmuir.0c01955 Text en © 2020 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes.
spellingShingle Sridharan, Simha
Meinders, Marcel B. J.
Bitter, Johannes H.
Nikiforidis, Constantinos V.
On the Emulsifying Properties of Self-Assembled Pea Protein Particles
title On the Emulsifying Properties of Self-Assembled Pea Protein Particles
title_full On the Emulsifying Properties of Self-Assembled Pea Protein Particles
title_fullStr On the Emulsifying Properties of Self-Assembled Pea Protein Particles
title_full_unstemmed On the Emulsifying Properties of Self-Assembled Pea Protein Particles
title_short On the Emulsifying Properties of Self-Assembled Pea Protein Particles
title_sort on the emulsifying properties of self-assembled pea protein particles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7586397/
https://www.ncbi.nlm.nih.gov/pubmed/32988196
http://dx.doi.org/10.1021/acs.langmuir.0c01955
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