{"title":"探讨植物化学皂苷在阻止α-乳清蛋白热聚集中的作用:多维光谱分析","authors":"Yutong Jiang , Xin Wen , Jiahui Guo , Hongyu Li , Zhanmei Jiang , Yun Chen","doi":"10.1016/j.foodhyd.2025.112029","DOIUrl":null,"url":null,"abstract":"<div><div>This study investigated how tea saponin (Ts), gypenoside (Gyp), mogroside V (Mog), glycyrrhizic acid (GA) and stevioside (STE) affected the heat-induced aggregates of α-lactalbumin (Ala), focusing on the inhibition mechanisms of disulfide cross-linking and their impact on structural and physicochemical properties. SDS-PAGE and size exclusion chromatography (SEC) confirmed that saponins probably bound Ala monomers via hydrophobic forces and hydrogen bonds, inhibiting the formation of disulfide bonds in heat-induced Ala (H-Ala) and effectively decreasing polymer generation, with the inhibitory effect in the order of Gyp, GA, Ts, STE, Mog. LC-MS/MS analysis revealed that Ala (6), Ala (91), Ala (111) and Ala (120) were the most active sites for the disulfide cross-linking reaction in H-Ala. Specifically, the number of intramolecular disulfide cross-linked peptides of heat-induced Ala-Mog, Ala-STE, Ala-GA, Ala-Ts and Ala-Gyp complexes significantly decreased by 5, 6, 7, 8 and 10, respectively, compared with H-Ala. Notably, the heat-induced Ala-Gyp complex exhibited the highest absolute zeta potential, smallest particle size, and lowest hydrophobicity, which correlated with its superior inhibition of aggregation. The study highlighted the potential of saponins as natural additives for the stabilization of heat-sensitive proteins during thermal processing, offering new insights for food industry applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112029"},"PeriodicalIF":11.0000,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Exploring the role of phytochemical saponins in preventing the thermal aggregation of α-lactalbumin: A multi-dimensional spectrometric analysis\",\"authors\":\"Yutong Jiang , Xin Wen , Jiahui Guo , Hongyu Li , Zhanmei Jiang , Yun Chen\",\"doi\":\"10.1016/j.foodhyd.2025.112029\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>This study investigated how tea saponin (Ts), gypenoside (Gyp), mogroside V (Mog), glycyrrhizic acid (GA) and stevioside (STE) affected the heat-induced aggregates of α-lactalbumin (Ala), focusing on the inhibition mechanisms of disulfide cross-linking and their impact on structural and physicochemical properties. SDS-PAGE and size exclusion chromatography (SEC) confirmed that saponins probably bound Ala monomers via hydrophobic forces and hydrogen bonds, inhibiting the formation of disulfide bonds in heat-induced Ala (H-Ala) and effectively decreasing polymer generation, with the inhibitory effect in the order of Gyp, GA, Ts, STE, Mog. LC-MS/MS analysis revealed that Ala (6), Ala (91), Ala (111) and Ala (120) were the most active sites for the disulfide cross-linking reaction in H-Ala. Specifically, the number of intramolecular disulfide cross-linked peptides of heat-induced Ala-Mog, Ala-STE, Ala-GA, Ala-Ts and Ala-Gyp complexes significantly decreased by 5, 6, 7, 8 and 10, respectively, compared with H-Ala. Notably, the heat-induced Ala-Gyp complex exhibited the highest absolute zeta potential, smallest particle size, and lowest hydrophobicity, which correlated with its superior inhibition of aggregation. The study highlighted the potential of saponins as natural additives for the stabilization of heat-sensitive proteins during thermal processing, offering new insights for food industry applications.</div></div>\",\"PeriodicalId\":320,\"journal\":{\"name\":\"Food Hydrocolloids\",\"volume\":\"172 \",\"pages\":\"Article 112029\"},\"PeriodicalIF\":11.0000,\"publicationDate\":\"2025-09-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Hydrocolloids\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0268005X25009890\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0268005X25009890","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
Exploring the role of phytochemical saponins in preventing the thermal aggregation of α-lactalbumin: A multi-dimensional spectrometric analysis
This study investigated how tea saponin (Ts), gypenoside (Gyp), mogroside V (Mog), glycyrrhizic acid (GA) and stevioside (STE) affected the heat-induced aggregates of α-lactalbumin (Ala), focusing on the inhibition mechanisms of disulfide cross-linking and their impact on structural and physicochemical properties. SDS-PAGE and size exclusion chromatography (SEC) confirmed that saponins probably bound Ala monomers via hydrophobic forces and hydrogen bonds, inhibiting the formation of disulfide bonds in heat-induced Ala (H-Ala) and effectively decreasing polymer generation, with the inhibitory effect in the order of Gyp, GA, Ts, STE, Mog. LC-MS/MS analysis revealed that Ala (6), Ala (91), Ala (111) and Ala (120) were the most active sites for the disulfide cross-linking reaction in H-Ala. Specifically, the number of intramolecular disulfide cross-linked peptides of heat-induced Ala-Mog, Ala-STE, Ala-GA, Ala-Ts and Ala-Gyp complexes significantly decreased by 5, 6, 7, 8 and 10, respectively, compared with H-Ala. Notably, the heat-induced Ala-Gyp complex exhibited the highest absolute zeta potential, smallest particle size, and lowest hydrophobicity, which correlated with its superior inhibition of aggregation. The study highlighted the potential of saponins as natural additives for the stabilization of heat-sensitive proteins during thermal processing, offering new insights for food industry applications.
期刊介绍:
Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication.
The main areas of interest are:
-Chemical and physicochemical characterisation
Thermal properties including glass transitions and conformational changes-
Rheological properties including viscosity, viscoelastic properties and gelation behaviour-
The influence on organoleptic properties-
Interfacial properties including stabilisation of dispersions, emulsions and foams-
Film forming properties with application to edible films and active packaging-
Encapsulation and controlled release of active compounds-
The influence on health including their role as dietary fibre-
Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes-
New hydrocolloids and hydrocolloid sources of commercial potential.
The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.