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在饮料模型体系中,预热乳清蛋白分离物与玫瑰花色苷提取物的相互作用:对颜色稳定性、涩味和机制的影响。

Interaction of preheated whey protein isolate with rose anthocyanin extracts in beverage model system: Influence on color stability, astringency and mechanism.

机构信息

State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.

The Food College of Shihezi University, Shihezi, Xinjiang 832003, China.

出版信息

Food Chem. 2023 Jun 30;412:135507. doi: 10.1016/j.foodchem.2023.135507. Epub 2023 Jan 18.

Abstract

Preheating proteins have the potential to improve anthocyanin stability. Our aim was to investigate the effect of preheated whey protein isolate (WPI) on the color stability and astringency of the beverage model system in the presence of rose anthocyanin extracts (RAEs), and to explore the mechanism of interaction between preheated WPI and RAEs. The secondary structure, particle size and transparency of WPI were obviously changed by preheating. WPI preheated at 100°C  (WPI100) could effectively improve the color stability of RAEs in the beverage model system. Importantly, the WPI100-RAEs in the beverage model system exhibited the smallest particle size and the weakest astringency effect. In addition, different preheated WPIs could interact with RAEs non-covalently, and the interaction forces are hydrogen bonding and van der Waals forces, among which WPI100 had the strongest binding ability to RAEs. These results will provide a new insight into the development of protein-anthocyanin beverages.

摘要

预热蛋白质有可能提高花色苷的稳定性。我们的目的是研究在含有玫瑰花色苷提取物(RAE)的饮料模型系统中,预热乳清蛋白分离物(WPI)对饮料颜色稳定性和涩味的影响,并探讨预热 WPI 和 RAE 之间相互作用的机制。WPI 的二级结构、粒径和透明度因预热而明显改变。在 100°C 下预热的 WPI(WPI100)可以有效地提高饮料模型系统中 RAE 的颜色稳定性。重要的是,饮料模型系统中的 WPI100-RAE 表现出最小的粒径和最弱的涩味效果。此外,不同预热的 WPIs 可以与 RAE 非共价相互作用,相互作用力是氢键和范德华力,其中 WPI100 与 RAE 具有最强的结合能力。这些结果将为开发蛋白质-花色苷饮料提供新的思路。

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