Search

This work investigated the effect of treatment of soy protein isolate (SPI) with basic amino acids (BAA) (l -Arginine, l -Histidine, and l -Lysine) at different concentrations prior to spray drying on the beany-flavor and functional properties. The results illustrated that the BAA prominently improved the solubility and emulsifying properties of SPI, and reduced the its release of beany-flavor compounds. Additionally, l -Arginine was more effective in increasing the solubility and emulsifying properties of the SPI than l -Histidine and l -Lysine. Notably, 0.3% l -Arginine improved the solubility, emulsifying activity index, emulsifying stability index of the SPI by 43.5%, 64.2% and 45.3% respectively. Through the headspace solid-phase microextraction gas chromatography-mass spectrometry (HS-SPME-GC-MS) and headspace-gas chromatography-ion mobility spectrometry (HS-GC-IMS), the 0.3% BAA showed the better mitigation effect on the beany flavor of SPI among three addition concentrations. The increased ζ-potential showed that BAA enhanced the electrostatic repulsion of the SPI, facilitating its dissolution and formation of a more stable emulsion system. Surface hydrophobicity and fluorescence spectral results revealed that BAA enhance the exposure of hydrophobic groups, enhancing the stability of oil-water interface and promoting the interaction between beany-flavor compounds and SPI. These findings lay the theoretical groundwork for further research and application of soy protein. [Display omitted] • Basic amino acids (BAA) increased the solubility of soy protein isolate (SPI). • BAA enhanced the emulsion activity/stability index of SPI. • BAA diminished the release intensity of beany flavor from SPI. • BAA improved the absolute value of potential and surface hydrophobicity of SPI. • BAA reduced the free sulfhydryl groups of SPI. [ABSTRACT FROM AUTHOR]

Interfacial deformation and interfacial rheology behaviour of prolamin particles are relevant factors affecting their emulsification performance but have not yet been paid considerable attention to. Based on the finding that CMC modification significantly improved the emulsifying property of gliadin colloid particles (GCPs), the present study combined in situ observation and interfacial rheology as a tool to investigate the effect of CMC on the structure characteristics, interfacial deformation and interfacial rheology behaviour of GCPs and their correlation with emulsifying performance. The results demonstrated that gliadin/CMC complex particles (GCCPs) presented looser core-shell structures than GCPs. The interfacial deformation of particles and the formation of smooth interfaces were observed for both GCPs and GCCPs, and GCCPs exhibited faster deformation behaviour, which should correlate to the looser structure. Although GCCPs showed lower surface pressure and viscoelasticity modulus, the existence of CMC promoted the initial adsorption of particles and accelerated the formation of viscoelastic interfacial films, which contributed to the improvement of emulsifying performance. In addition, CMC endowed the interfacial layers with moderate viscosity and fluidity to resist the destabilisation induced by oil droplet deformation. The present study should provide insights for intuitive understanding and fine regulation of the interfacial behaviour of protein particles. • Gliadin/CMC complex particles present a relatively "softer" core-shell structure. • "Softer" structure is easier to unfold and deform at the oil-water interface. • Faster interfacial deformation of particles benefits the emulsifying performance. • CMC promotes the initial adsorption and accelerates the formation of interface layers. • Moderate interfacial viscosity and fluidity facilitates the stability of oil droplets. [ABSTRACT FROM AUTHOR]