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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2020
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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. |
format | Online Article Text |
id | pubmed-7586397 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
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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