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  • Title: Stability Mechanism of Two Soybean Protein-Phosphatidylcholine Nanoemulsion Preparation Methods from a Structural Perspective: A Raman Spectroscopy Analysis.
    Author: Zhu Y, Li Y, Wu C, Teng F, Qi B, Zhang X, Zhou L, Yu G, Wang H, Zhang S, Wang Z, Jiang L.
    Journal: Sci Rep; 2019 May 06; 9(1):6985. PubMed ID: 31061497.
    Abstract:
    Ultrasound treatment and high-pressure homogenization were used to prepare soybean protein (SP)-phosphatidylcholine (PC) nanoemulsions in this study. Nanoemulsions prepared by high-pressure homogenization were more stable. The structural changes of SP and PC under ultrasound treatment and high-pressure homogenization treatment were investigated by Raman spectroscopy. It could be concluded that ultrasound and high-pressure homogenization treatments increased both the content of α-helix and unordered structure but decreased that of β-structures of SP, while the interaction between SP and PC decreased α-helix content and also reduced unordered structure and β-sheet structure. Ultrasound treatment and high-pressure homogenization exposed more tryptophan and tyrosine residues to promote hydrophobic interaction between SP and PC, which was beneficial for stabilizing the nanoemulsion. The SP-PC interaction exerted a more significant effect on side chain structure than those observed under ultrasound treatment and high-pressure homogenization. The dominant g-g-t vibrational mode of the disulfide bond of soybean protein was not appreciably changed by the two preparations. High-pressure homogenization increased the disorder of lipid chains of PC, promoting SP-PC interaction and thereby increasing the stability of the nanoemulsion. The structural change provided a theoretical basis for preparation of two nanoemulsions.
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