“…; Gao et al . ). Solubility, aggregates, structure, surface hydrophobicity, and foaming and emulsifying properties of native soy proteins (i.e., β‐conglycinin and glycinin) may be affected by heat treatments.…”
Section: Resultsmentioning
confidence: 97%
“…However, heat treatment of almost completely denatured soy proteins also affected some of their physical and functional properties Native soybean protein has a highly ordered, compact and collapsed globular structure, and most functional groups (such as amides, hydroxyls and carboxyls) are buried within globular particles (Van der Leeden et al 2000), resulting in low solubility. In addition, soybean proteins have complicated and diverse primary, secondary, tertiary and quaternary structures, which are mainly built by weak intermolecular interactions including hydrogen bonds, electrostatic bonds, Van der Waals forces, disulfide bonds and hydrophobic interactions, which lead to low reactivity (Fahmy et al 2010;Gao et al 2015). Solubility, aggregates, structure, surface hydrophobicity, and foaming and emulsifying properties of native soy proteins (i.e., b-conglycinin and glycinin) may be affected by heat treatments.…”
Commercial soy protein isolates (SPIs; China 980A, China 880, ISP 974 and ADM 974) and soy protein concentrates (SPCs; SPC 700 and ARCON S) were used for comparing the effects of heat treatment (55C and 85C for 10–30 min) on the surface tension, surface hydrophobicity, viscosity, solubility at pH 3–8 and foaming properties. The foam capacity was highly positively correlated with the surface hydrophobicity, but negatively related to the surface tension, liquid percentage and foam maximum density. Heating commercial SPIs and SPCs improved the foam capacity, changed the surface hydrophobicity, solubility, foam maximum density and foam stability, and decreased the surface tension and viscosity. The heating temperatures had a greater influence on protein properties than did the heating time. Among soy protein products, heat‐modified China 980A had the best foam capacity and foam stability.
Practical Applications
Simple heating treatments improved foaming properties of commercial soy products with low level of surface tension and high level of surface hydrophobicity and solubility. In particular, heating improved surface tension, foaming capacity, liquid percentage, foam maximum density and not damaged foaming stability in most of samples. These results indicate that a relatively inexpensive, high quality foaming properties was obtained by the action of heating process that benefits the application of using commercial soy proteins as foaming agents in aerated food systems. Therefore, the foaming properties of heated soy proteins were dramatically different, showing great potential for improving tailor‐made proteins for various applications.
“…; Gao et al . ). Solubility, aggregates, structure, surface hydrophobicity, and foaming and emulsifying properties of native soy proteins (i.e., β‐conglycinin and glycinin) may be affected by heat treatments.…”
Section: Resultsmentioning
confidence: 97%
“…However, heat treatment of almost completely denatured soy proteins also affected some of their physical and functional properties Native soybean protein has a highly ordered, compact and collapsed globular structure, and most functional groups (such as amides, hydroxyls and carboxyls) are buried within globular particles (Van der Leeden et al 2000), resulting in low solubility. In addition, soybean proteins have complicated and diverse primary, secondary, tertiary and quaternary structures, which are mainly built by weak intermolecular interactions including hydrogen bonds, electrostatic bonds, Van der Waals forces, disulfide bonds and hydrophobic interactions, which lead to low reactivity (Fahmy et al 2010;Gao et al 2015). Solubility, aggregates, structure, surface hydrophobicity, and foaming and emulsifying properties of native soy proteins (i.e., b-conglycinin and glycinin) may be affected by heat treatments.…”
Commercial soy protein isolates (SPIs; China 980A, China 880, ISP 974 and ADM 974) and soy protein concentrates (SPCs; SPC 700 and ARCON S) were used for comparing the effects of heat treatment (55C and 85C for 10–30 min) on the surface tension, surface hydrophobicity, viscosity, solubility at pH 3–8 and foaming properties. The foam capacity was highly positively correlated with the surface hydrophobicity, but negatively related to the surface tension, liquid percentage and foam maximum density. Heating commercial SPIs and SPCs improved the foam capacity, changed the surface hydrophobicity, solubility, foam maximum density and foam stability, and decreased the surface tension and viscosity. The heating temperatures had a greater influence on protein properties than did the heating time. Among soy protein products, heat‐modified China 980A had the best foam capacity and foam stability.
Practical Applications
Simple heating treatments improved foaming properties of commercial soy products with low level of surface tension and high level of surface hydrophobicity and solubility. In particular, heating improved surface tension, foaming capacity, liquid percentage, foam maximum density and not damaged foaming stability in most of samples. These results indicate that a relatively inexpensive, high quality foaming properties was obtained by the action of heating process that benefits the application of using commercial soy proteins as foaming agents in aerated food systems. Therefore, the foaming properties of heated soy proteins were dramatically different, showing great potential for improving tailor‐made proteins for various applications.
“…The addition of this powder could also conveniently and effectively increase the solid content of the soybean protein adhesive to 60 wt %, which was comparable to that of commercial UF adhesive (commonly 50–65 wt %). The test results in Table confirmed that TSP could apparently improve the water resistance of crosslinker‐modified soybean protein adhesive because the soybean protein post‐thermal acid treatment had an increased boiling water‐insoluble network structure …”
Section: Resultsmentioning
confidence: 99%
“…Our previous study showed that thermal acid treatment could improve the water resistance of soybean proteins due to the formation of the water‐resistant intermolecular network during treatment . Literature review also indicated that crosslinking could significantly improve the water resistance of soybean protein adhesive due to the formation of chemical network between proteins . Therefore, the current study attempts to develop a novel soybean protein adhesive with good water resistance and technological applicability through the combination of thermal alkali degradation, thermal acid treatment, and crosslinking modification.…”
“…Xu et al reported that the water resistance of soy protein adhesives was improved by appropriate succinylation or PAE cross‐linking. Gao et al showed the positive effect of cross linker species on the water resistance of soy adhesive. In addition, Liu and Li found maleic anhydride to have negative effects on adhesion performance of soy protein.…”
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