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• W1975930491 abstract "Systematically characterizing soymilk protein is important for understanding the formation of soymilk-related products and may be beneficial for enhancing the qualities of these products. Field emission scanning electron microscopy showed that soymilk protein could be divided into three categories: large (40–258 nm) and small (20–40 nm) stable protein particles and <20 nm soluble proteins. Regardless of soybean variety, the large protein particles contained lipoxygenase, γ-conglycinin, lectin, and Kunitz trypsin inhibitor as well as glycinin and β-conglycinin. These large protein particles were comprised of 40-nm protein aggregates (around 40 nm) formed by heat-dissociated soybean protein subunits. In addition, the small stable protein particles, which accounted for about 10% of soymilk protein, increased with β subunits of β-conglycinin while the soluble proteins (<20 nm) existed as monomers and oligomers of α′, α and acidic polypeptides." @default.
• W1975930491 created "2016-06-24" @default.
• W1975930491 creator A5024369471 @default.
• W1975930491 creator A5065397968 @default.
• W1975930491 date "2014-08-01" @default.
• W1975930491 modified "2023-10-14" @default.
• W1975930491 title "Protein particle and soluble protein structure in prepared soymilk" @default.
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• W1975930491 doi "https://doi.org/10.1016/j.foodhyd.2014.01.005" @default.
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