Interaction and phase behavior of whey protein and propylene glycol alginate complex condensates
文献类型： 外文期刊
作者： Shi, Ge 1 ; Shi, Ce 3 ; Luo, Yongkang 1 ; Hong, Hui 1 ; Zhang, Jiaran 3 ; Li, Yan 1 ; Tan, Yuqing 1 ;
作者机构： 1.China Agr Univ, Coll Food Sci & Nutr Engn, Beijing Lab Food Qual & Sfety, Beijing 100083, Peoples R China
2.China Agr Univ, Coll Food Sci & Nutr Engn, Ctr Food Colloids & Delivery Funct, Beijing 100083, Peoples R China
3.Beijing Acad Agr & Forestry Sci, Informat Technol Res Ctr, Beijing 100097, Peoples R China
4.Beijing Acad Agr & Forestry Sci, Natl Engn Res Ctr Informat Technol Agr, Beijing 100097, Peoples R China
5.Beijing Acad Agr & Forestry Sci, Natl Engn Lab Agriprod Qual Traceabil, Beijing 100097, Peoples R China
关键词： Whey protein; Propylene glycol alginate; Phase behavior; Coacervate; Interaction
期刊名称：FOOD CHEMISTRY （ 影响因子：8.8； 五年影响因子：8.6 ）
ISSN： 0308-8146
年卷期： 2023 年 404 卷
页码：
收录情况： SCI
摘要： Whey protein (WP) is ubiquitously applied in food products, but its sensitivity to food processing conditions has limited its application. Herein, we chose propylene glycol alginate (PGA) to combine with WP to enhance its stability. The ideal ratio of WP/PGA for coacervation was 3:1, and the soluble complex and insoluble complex were formed at pH 5.2 (pHc) and pH 4.4 (pH phi 1) at this ratio, respectively. The UV absorption spectra, fluo-rescence spectra, and XRD results revealed that the interaction between PGA and WP changed the tertiary conformation of WP. The FTIR and molecular docking results suggested electrostatic interactions, hydrogen bonding and hydrophobic interactions were all involved in the formation of WP-PGA complexes, and the thermal stability of WP was improved based on the DSC results. These findings supported PGA to keep dairy products stable and transparent at the isoelectric point and WP-PGA complexes could be applied in encapsulating bioactive substances.
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