Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt Concentrations
The protein transition motivates the use of plant proteins, but their application in food emulsions is challenging, especially when high concentrations of oil and salt are needed for formulation and sensory properties. In the present work, we connect the iso-electric point of two potato protein isol...
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MDPI AG
2024-11-01
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| Series: | Foods |
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| author | Jiarui Cao Meinou Corstens Karin Schroën |
| author_facet | Jiarui Cao Meinou Corstens Karin Schroën |
| author_sort | Jiarui Cao |
| collection | DOAJ |
| description | The protein transition motivates the use of plant proteins, but their application in food emulsions is challenging, especially when high concentrations of oil and salt are needed for formulation and sensory properties. In the present work, we connect the iso-electric point of two potato protein isolates (patatin-rich, POPI-200; protease inhibitor-rich, POPI-300) and a faba protein isolate (FPI) to the behavior in the bulk phase and at the interface, and relate this to the physical stability of 45 wt% oil-in-water (O/W) emulsions in the presence of NaCl at pH 4.0–7.0. In the absence of NaCl, a higher bulk viscosity was found at the iso-electric point (IEP), especially for the FPI. In the presence of NaCl, the viscosity of the POPI-200 solutions was highest, followed by POPI-300, and that of the FPI was lowest, irrespective of the pH. Both POPIs showed faster initial adsorption at the O/W interface in the absence of NaCl, and formed a more elastic layer compared to the FPI. For all proteins, salt addition leads to less elastic films. Interestingly, the interfaces were more elastic at a pH close to the IEP of the protein in the presence of NaCl. Both POPI-stabilized emulsions showed higher stability (smaller size and less oiling off) than the FPI-stabilized emulsions, which makes potato proteins relevant for food emulsion product formulation, even under high salt conditions. |
| format | Article |
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| institution | DOAJ |
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| language | English |
| publishDate | 2024-11-01 |
| publisher | MDPI AG |
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| series | Foods |
| spelling | doaj-art-00ec6291a557486a8682c6e1e25d49da2025-08-20T02:50:38ZengMDPI AGFoods2304-81582024-11-011323379510.3390/foods13233795Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt ConcentrationsJiarui Cao0Meinou Corstens1Karin Schroën2Laboratory of Food Process Engineering, Wageningen University and Research, Bornse Weilanden 9, 6708 WG Wageningen, The NetherlandsLaboratory of Food Process Engineering, Wageningen University and Research, Bornse Weilanden 9, 6708 WG Wageningen, The NetherlandsLaboratory of Food Process Engineering, Wageningen University and Research, Bornse Weilanden 9, 6708 WG Wageningen, The NetherlandsThe protein transition motivates the use of plant proteins, but their application in food emulsions is challenging, especially when high concentrations of oil and salt are needed for formulation and sensory properties. In the present work, we connect the iso-electric point of two potato protein isolates (patatin-rich, POPI-200; protease inhibitor-rich, POPI-300) and a faba protein isolate (FPI) to the behavior in the bulk phase and at the interface, and relate this to the physical stability of 45 wt% oil-in-water (O/W) emulsions in the presence of NaCl at pH 4.0–7.0. In the absence of NaCl, a higher bulk viscosity was found at the iso-electric point (IEP), especially for the FPI. In the presence of NaCl, the viscosity of the POPI-200 solutions was highest, followed by POPI-300, and that of the FPI was lowest, irrespective of the pH. Both POPIs showed faster initial adsorption at the O/W interface in the absence of NaCl, and formed a more elastic layer compared to the FPI. For all proteins, salt addition leads to less elastic films. Interestingly, the interfaces were more elastic at a pH close to the IEP of the protein in the presence of NaCl. Both POPI-stabilized emulsions showed higher stability (smaller size and less oiling off) than the FPI-stabilized emulsions, which makes potato proteins relevant for food emulsion product formulation, even under high salt conditions.https://www.mdpi.com/2304-8158/13/23/3795plant proteinbulk viscosityO/W interfaceinterfacial rheologyemulsionsphysical stability |
| spellingShingle | Jiarui Cao Meinou Corstens Karin Schroën Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt Concentrations Foods plant protein bulk viscosity O/W interface interfacial rheology emulsions physical stability |
| title | Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt Concentrations |
| title_full | Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt Concentrations |
| title_fullStr | Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt Concentrations |
| title_full_unstemmed | Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt Concentrations |
| title_short | Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt Concentrations |
| title_sort | interfacial and bulk properties of potato and faba protein in connection with physical emulsion stability at various ph values and high salt concentrations |
| topic | plant protein bulk viscosity O/W interface interfacial rheology emulsions physical stability |
| url | https://www.mdpi.com/2304-8158/13/23/3795 |
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