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Updated: Oct 10, 2025

Designing Silk-silk Protein Alloy Materials for Biomedical Applications
Published on: August 13, 2014
Fabrication and emulsifying properties of non-covalent complexes between soy protein isolate fibrils and soy soluble
Hekai Zhao1, Shengnan Wang1,2, Guilan Zhao1
1College of Food Science and Technology, Bohai University, Jinzhou, 121013, China. 13072615294@163.com.
Abstract:
Non-covalent complexes (SPIF/SSPS) of soy protein isolate fibrils (SPIF) and soy soluble polysaccharides (SSPS) were fabricated and used to stabilize oil-in-water (O/W) emulsions. FT-IR spectroscopy and zeta potential results demonstrated that the interactions between SPIF and SSPS mainly include hydrogen bonding and electrostatic interactions. The presence of SSPS decreased the particle size and surface hydrophobicity of SPIF, resulting in a decrease and redshift of the fluorescence intensity. During the interfacial adsorption process, SPIF/SSPS complexes had lower diffusion and penetration rates compared with pure SPIF because of their hydrophilic region, but the molecular reorganization rate increased. Emulsions stabilized with the SPIF/SSPS complex at 5 : 5 (i.e., 1 : 1) ratio had both an excellent emulsifying activity index (EAI) of 26.17 m2 g-1 and an excellent emulsifying stability index (ESI) of 93.01%, as well as the smallest emulsion droplet particle size of 1.74 μm. Meanwhile, no flocculation was observed in this emulsion which is attributed to the sufficient steric stabilization provided by the hydrophilic SSPS. After three weeks of storage, there was no phase separation observed in the emulsions stabilized by SPIF/SSPS complexes in 5 : 4 and 5 : 5 ratios and the Turbiscan stability indices were 17.86 and 15.14, respectively, much lower than the other emulsion formulations tested.
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