1. pH-induced physiochemical and structural changes of milk proteins mixtures and its effect on foaming behavior.
- Author
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Zhang, Siyu, Hao, Junli, Xie, Qinggang, Pi, Xiaowen, Peng, Zeyu, Sun, Yuxue, and Cheng, Jianjun
- Subjects
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FOAM , *MILK proteins , *PEARSON correlation (Statistics) , *WHEY proteins , *MIXTURES , *SURFACE pressure , *PROTEIN structure - Abstract
Milk proteins are well known to produce aerated food due to the amphiphilicity. However, milk proteins are commonly added in blends for the desirable properties in food industry. In this study, the foaming properties of milk protein mixtures (MPM), a mixtures of whey protein isolated (WPI) and milk protein concentrate (MPC), was studied through foaming capacity (FC), foam stability (FS), and foam morphology at pH 3.0–9.0. Physiochemical, structural, surface properties, and Pearson correlation analysis were measured to gain insight into foaming behavior. Results indicated that MPM showed excellent FC (113.0–114.3 %) and FS (90.7–93.0 %) at pH 6.0–9.0, and foam displayed a smaller size and uniform distribution. MPM solutions showed smaller particles, higher solubility, and lower apparent viscosity at pH 6.0–9.0, which resulted in an increase in surface pressure and adsorption rate (K diff), facilitating more protein absorbed to interface. To further investigate structural changes, various spectral methods were used, in which the structure of MPM was changed with pH. Correlation analysis further suggests that K diff and solubility positively affect the formation of foam, while free sulfhydryl and β -sheet contributed to stabilizing foams. These findings provide valuable information on MPM as ingredients for aerated foods under acidic, neutral, and alkaline conditions. • Foaming properties of milk proteins mixtures were varied at different pH values. • Milk proteins mixtures showed higher foaming properties at pH 6.0–9.0. • Milk proteins mixtures showed the lowest FC and FS at pH 5.0 and 3.0. • FC was positively correlated with K diff , solubility, and H 0. • FS was highly related to protein structure and interaction between proteins. [ABSTRACT FROM AUTHOR]
- Published
- 2024
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