分离乳清蛋白粉
牛血清白蛋白
化学
抗氧化剂
食品科学
乳清蛋白
体外
生物化学
色谱法
作者
Zhihuan Zang,Shurui Chou,Lin Geng,Xu Si,Yumeng Ding,Yuxi Lang,Hong Cui,Ningxuan Gao,Yi Chen,Mingshuang Wang,Xu Xie,Bin Xue,Li B,Jinlong Tian
标识
DOI:10.1016/j.lwt.2021.112269
摘要
The interaction of proteins with anthocyanins (ACNs) gives rise to significant improvements in their functional properties. To explore the interactions between whey protein isolate (WPI)/bovine serum albumin (BSA) and blueberry ACNs, light (5000 Lux, 7 days), heat (85 °C, 2 h), sucrose (0.25 mg/mL), and vitamin C (0.15 mg/mL) were used to accelerate the degradation of ACNs. Through the observation of color changes and variations in the free radical scavenging rates, WPI and BSA were found to protect the ACNs to varying degrees. Moreover, WPI/BSA exhibited increased solubilities, foaming and emulsifying properties, and changed thermal stabilities and protein structures, in addition to decreased surface hydrophobicities and zeta potentials. Furthermore, the addition of WPI/BSA increased the number of ACN monomers in a simulated digestion system, as determined by high-performance liquid chromatography-mass spectrometry. Therefore, by studying the interactions between proteins and ACNs, we can provide a strategy and theoretical basis for determining the steady-state of ACNs in blueberry products.
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