scholarly journals Kinetic investigation of emulsion stability in oil/water emulsions stabilized with protein

2018 ◽  
Vol 1 (1) ◽  
pp. 21
Author(s):  
Vanya Gandova
Keyword(s):  
Soybean Oil ◽  
High Stability ◽  
Emulsion Stability ◽  
Soybean Protein ◽  
Optical Microscope ◽  
Kinetic Investigation ◽  
Protein Isolates ◽  
Ph Values ◽  
Soybean Protein Isolates ◽  
Oil Water

The emulsion stability soybean oil/water (O/W) with different concentrations was investigated. The dynamics of emulsion stabilities were investigated at 1 to 15 days as measured of turbidity. Three series of samples were prepared with 2 %, 4 %  and 5 % soybean protein isolates (SI). Obtained results were compared with other obtained with optical microscope. It was found that emulsions exhibited more stability in samples with 2 % SI. The pH was measured in all emulsions. pH interval was between 5.8–7.4and after analysis were seen that emulsions exhibited high stability around 7.2-7.3 pH values.

DSC study on the thermal properties of soybean protein isolates/corn starch mixture

2013 ◽  
Vol 115 (2) ◽  
pp. 1633-1638 ◽  
Author(s):  
Shujing Li ◽  
Yimin Wei ◽  
Yanqiang Fang ◽  
Wei Zhang ◽  
Bo Zhang
Keyword(s):  
Thermal Properties ◽  
Corn Starch ◽  
Soybean Protein ◽  
Protein Isolates ◽  
Soybean Protein Isolates

scholarly journals Hydration Properties of Soybean Protein Isolates

2001 ◽  
Vol 44 (4) ◽  
pp. 425-431 ◽  
Author(s):  
G. Remondetto ◽  
M. C. Añon ◽  
Rolando J. González
Keyword(s):  
Protein Denaturation ◽  
Soybean Protein ◽  
Sodium Dodecyl ◽  
High Water ◽  
Hydration Properties ◽  
Solubility In Water ◽  
Protein Isolates ◽  
Hydrodynamic Behaviour ◽  
Soybean Protein Isolates ◽  
Power Law Equation

Hydration properties of soybean isolates with different processing conditions (heat treatments, pH and protein concentrations) were studied. Degree of denaturation,, solubility in water, in 0.2mol/L NaCl, and in media of different sodium dodecyl sulfate concentrations, viscosity and water imbibing capacity of the different samples were determinated and correlated. Treatments at temperatures higher than 80ºC denatured 11S and 7S proteins, leading to exposure of hydrophobic groups, which produced insoluble aggregates either in water or in high ionic strength media. These isolates possessed high water imbibing capacities and gave rise to viscous dispersions. Significant correlations were obtained between hydration properties and the "m" coefficient as calculated by a power law equation relating viscosity with the protein concentration of the dispersion. This "m" coefficient also correlated with the denaturation enthalpy of the protein isolates. On the basis of these results, it might be suggested that the "m" coefficient - dependent of the hydrodynamic behaviour of the particles - was a good estimator of the degree of protein denaturation.

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