Abstract

Soy protein isolate (SPI) could be used as an emulsifier to stabilize emulsions, while SPI is unstable under low acidic conditions. The stable composite particles of SPI and dextran sulfate (DS) could be formed by the electrostatic interaction at the pH was 3.5. And the SPI/DS composite particles were used to prepare the high complex concentration emulsion. The stabilization properties of high complex concentration emulsion were investigated. Compared to uncompounded SPI, the particle size of SPI/DS composite particles was smaller at 1.52 μm, and the absolute value of the potential increased to 19.9 mV when the mass ratio of SPI to DS was 1:1 and the pH was 3.5. With the DS ratio increased, the solubility of the composite particles increased to 14.44 times of the untreated protein at pH 3.5, while the surface hydrophobicity decreased. Electrostatic interactions and hydrogen bonds were the main forces between SPI and DS, and DS was electrostatically adsorbed on the surface of SPI. The emulsion stability significantly enhanced with the increase of complex concentration (38.88 times higher than at 1% concentration), the emulsion average droplet size was the lowest (9.64 μm), and the absolute value of potential was the highest (46.67 mV) when the mass ratio of SPI to DS was 1:1 and the complex concentration of 8%. The stability of the emulsion against freezing was improved. The SPI/DS complex has high solubility and stability under low acidic conditions, and the SPI/DS complex' emulsion has a well stability. This article is protected by copyright. All rights reserved.

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