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pH-induced physiochemical and structural changes of milk proteins mixtures and its effect on foaming behavior.
Zhang, Siyu; Hao, Junli; Xie, Qinggang; Pi, Xiaowen; Peng, Zeyu; Sun, Yuxue; Cheng, Jianjun.
Afiliação
  • Zhang S; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Hao J; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Xie Q; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China; HeiLongJiang FeiHe Dairy Co., Ltd., Beijing 100015, China.
  • Pi X; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Peng Z; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Sun Y; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China. Electronic address: yuxue20@neau.edu.cn.
  • Cheng J; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China. Electronic address: jjcheng@neau.edu.cn.
Int J Biol Macromol ; 254(Pt 2): 127838, 2024 Jan.
Article em En | MEDLINE | ID: mdl-37923034
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 (Kdiff), 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 Kdiff and solubility positively affect the formation of foam, while free sulfhydryl and ß-sheet contributed to stabilizing foams. These findings provide valuable information on MPM as ingredients for aerated foods under acidic, neutral, and alkaline conditions.
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Texto completo: 1 Bases de dados: MEDLINE Assunto principal: Proteínas do Leite Idioma: En Revista: Int J Biol Macromol Ano de publicação: 2024 Tipo de documento: Article País de afiliação: China

Texto completo: 1 Bases de dados: MEDLINE Assunto principal: Proteínas do Leite Idioma: En Revista: Int J Biol Macromol Ano de publicação: 2024 Tipo de documento: Article País de afiliação: China