Effects of pH, Electrolyte Concentrations, and Alginate Molecular Weights on Surface Hydrophobicity of Soy Protein Isolates

2016 ◽  
Vol 45 (9) ◽  
pp. 1285-1292
Author(s):  
Yeong-Seon Lim ◽  
Byung-Jin Yoo
2000 ◽  
Vol 6 (5) ◽  
pp. 407-414 ◽  
Author(s):  
L.G. Santiago ◽  
A.G. Bonaldo ◽  
R.J. González

This work evaluated the formation and stability of emulsions prepared with three soy protein iso lates with different sulfhydryl content (SHL) and at two different pHs (6.00 and 7.00). Solubility (Sol), emulsifying activity index (IAE), coalescence (%Coal), surface concentration of proteins (r), and ki netics of the creaming process were determined. The effects of pH and sample types or their interac tion were significant (p < 0.05) for the four variables. IAE was little enhanced by the SHL increment, while stability to coalescence decreased. Also, it was verified that Γ is negatively affected by the SHL increment. The pH effect on IAE depended on the SHL. When pH decreased, %Coale lowered and Γ increased. Emulsions destabilized by the floculation-creaming mechanism more slowly at pH 6.00 than at pH 7.00.


2012 ◽  
Vol 554-556 ◽  
pp. 944-948 ◽  
Author(s):  
Lin Chen ◽  
Jian She Chen ◽  
Lin Yu ◽  
Ke Gang Wu ◽  
Xiao Li Liu ◽  
...  

Soy protein isolates (SPI) were modified by ultrasound treatment (200W, 400W, 600W), and the emulsifying properties of USPI (ultrasound treated SPI) were investigated. Analysis of mean droplet sizes and creaming indices of emulsions (20% v/v oil, 1.6% w/v emulsifier) formed by control SPI and USPI-200−600W showed that ultrasound treatment could improve the emulsifying capability and emulsion stabilizing ability (against creaming) of SPI. And the improvements were significantly influenced by the power level of ultrasound. Some USPI (e.g., 400W) was capable of producing stable fine emulsions. A variety of physicochemical and interfacial properties of USPI in relation to emulsifying properties have been investigated. The results showed that compared with control SPI, USPI-400W had a higher protein adsorption fraction (Fads) and a lower saturation surface load (Гsat), which was mainly due to its higher PS and surface hydrophobicity (H0), and may explain its markedly improved emulsifying capability. This study showed that ultrasound treatment could be an effective way for the functionality modification of globular proteins.


2003 ◽  
Vol 56 (4) ◽  
pp. 331-338 ◽  
Author(s):  
Germán Jovanovich ◽  
Marı́a C Puppo ◽  
Sergio A Giner ◽  
Marı́a C Añón

2018 ◽  
Vol 192 ◽  
pp. 193-201 ◽  
Author(s):  
Wenjie Wang ◽  
Mingyue Shen ◽  
Suchen Liu ◽  
Lian Jiang ◽  
Qianqian Song ◽  
...  

2020 ◽  
Vol 100 ◽  
pp. 105395 ◽  
Author(s):  
Jian He ◽  
Ren Wang ◽  
Wei Feng ◽  
Zhengxing Chen ◽  
Tao Wang

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