Morphology of soy protein isolate at oil/water and oil/air interfaces

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Abstract

Herein,the emulsifying properties of soy protein isolate (SPI) were highlighted by showing that the macromolecules undergo conformational changes when adsorbed at interfaces. The conformation of protein chains nested at the interfacial region of oil in water (o/w) emulsions by means of X-ray scattering (SAXS) and direct imaging (scanning electron microscopy (SEM)) techniques was investigated. The mean radius of gyration (Rg) for SPI (aq) is 20 nm and increases up to 30 nm in o/w emulsions; the proteins act as amphiphilic molecules by exposing their hydrophobic core to the oil and their hydrophilic amino acid residues to the water phase. By spray drying the emulsions,it was also possible to measure the size (Rg = 40 nm) and to evaluate the morphology of these proteins at the oil/air interface of the respective microcapsules. The walls of microcapsules are fractals of clustered objects with rough surfaces,which are smoothed by the presence of a cross-linking agent. © 2013 Sociedade Brasileira de Química.

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APA

Fayad, S. J., Zanetti-Ramos, B. G., Barreto, P. L. M., Soldi, V., & Minatti, E. (2013). Morphology of soy protein isolate at oil/water and oil/air interfaces. Journal of the Brazilian Chemical Society, 24(6), 1012–1017. https://doi.org/10.5935/0103-5053.20130130

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