Description
This dataset contains raw and processed experimental data on the bulk properties, interfacial behavior, and emulsion stability stabilized by of two potato protein isolates (patatin-rich, POPI-200; protease inhibitor-rich, POPI-300) and faba protein isolate (FPI) at various pH and high salt concentration.
The data are organized into five folders: Article, Protein characterization, Bulk viscosity, Oil-water interface, and Emulsion characterization. Each folder includes Excel files with raw measurements and processed data. Origin project files used for data visualization and figure preparation are also included.
Data collection was performed using multiple analytical techniques. The denatured state and thermal properties (denaturation temperature (Td) and enthalpy change (ΔH)) of the plant proteins were determined by differential scanning calorimetry (DSC-250, Mettler Toledo, Schwerzenbach, Switzerland). Protein characterization measurements included zata potential and particle size analysis using the Zetasizer Ultra, protein solubility was measured using BCA assay, and surface hydrophobicity measurements using the Shimadzu RF6000 Fluorimeter. Bulk viscosity was measured using an Anton Paar Rheometer MCR 702. Interfacial adsorption kinetics and interfacial rheology were measured using the TRACKER™ Automatic Drop Tensiometer (ADT) and Dilatational Interfacial Rheometer (Teclis, Civrieux-d’Azergues, France). Droplet size distribution of oil-in-water emulsion was measured using Mastersizer 3000. wereExperimental conditions include different protein concentrations and heat-treatment temperatures. Regarding the protein surface load, gravitational separation of emulsion droplets, and emulsion morphology, more details are described in the associated article "Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt Concentrations.
The data are organized into five folders: Article, Protein characterization, Bulk viscosity, Oil-water interface, and Emulsion characterization. Each folder includes Excel files with raw measurements and processed data. Origin project files used for data visualization and figure preparation are also included.
Data collection was performed using multiple analytical techniques. The denatured state and thermal properties (denaturation temperature (Td) and enthalpy change (ΔH)) of the plant proteins were determined by differential scanning calorimetry (DSC-250, Mettler Toledo, Schwerzenbach, Switzerland). Protein characterization measurements included zata potential and particle size analysis using the Zetasizer Ultra, protein solubility was measured using BCA assay, and surface hydrophobicity measurements using the Shimadzu RF6000 Fluorimeter. Bulk viscosity was measured using an Anton Paar Rheometer MCR 702. Interfacial adsorption kinetics and interfacial rheology were measured using the TRACKER™ Automatic Drop Tensiometer (ADT) and Dilatational Interfacial Rheometer (Teclis, Civrieux-d’Azergues, France). Droplet size distribution of oil-in-water emulsion was measured using Mastersizer 3000. wereExperimental conditions include different protein concentrations and heat-treatment temperatures. Regarding the protein surface load, gravitational separation of emulsion droplets, and emulsion morphology, more details are described in the associated article "Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt Concentrations.
| Date made available | 28 Jul 2026 |
|---|---|
| Publisher | Wageningen University & Research |
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