Ting-qi Yang , Kaiyu Jiang , Juncai Tu , Yuxuan Liang , Menghui Wang , Beiwei Zhu , Wei Gong
{"title":"α, β-不饱和醛诱导的乳蛋白修饰和多相食品系统中多酚干预的界面效应的新见解","authors":"Ting-qi Yang , Kaiyu Jiang , Juncai Tu , Yuxuan Liang , Menghui Wang , Beiwei Zhu , Wei Gong","doi":"10.1016/j.foodhyd.2025.111962","DOIUrl":null,"url":null,"abstract":"<div><div>Lipid peroxidation remains an inevitable challenge during dairy processing and storage. The α, β-unsaturated aldehydes produced during lipid peroxidation are highly reactive with proteins, which can degrade the stability and nutritional quality of dairy products. Polyphenols are widely used as antioxidants to control degradation caused by α, β-unsaturated aldehydes. However, most studies focus on homogeneous systems, overlooking the influence of the complex interfaces inherent in dairy products on protein modification by α, β-unsaturated aldehydes and the intervention of polyphenols. Herein, we established a Hex-milk protein interfacial model system and employed clickable probes (yne-ACR) to simulate the modification of milk proteins by α, β-unsaturated aldehydes. Additionally, six polyphenols with different structures were added to intervene the modification by yne-ACR. Results demonstrated that both yne-ACR modification and the intervention of different polyphenols significantly altered the dynamic interfacial behavior and expansion rheological properties of milk proteins. However, the impact on the stability of the interface model system was minimal. Notably, casein in milk proteins predominantly adsorbed at the interface. The in-gel fluorescence imaging revealed that the presence of the interface enhanced the modification of milk proteins by yne-ACR. The intervention effects of polyphenols varied based on their structural characteristics: PA, GA, GeA, RA, and EC inhibited the modification of non-adsorbed β-lactoglobulin (β-Lg) by yne-ACR, while EGCG significantly suppressed yne-ACR modification of both interfacial and non-adsorbed proteins and notably reduced protein carbonylation. This study highlights the critical role of interface microenvironment in influencing α, β-unsaturated aldehyde-protein interactions and analyzes the intervention effects of polyphenols with varying structures in complex food systems. These findings provide a theoretical foundation for the rational use of antioxidant strategies in dairy processing.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111962"},"PeriodicalIF":11.0000,"publicationDate":"2025-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Novel insights into interfacial effects on α, β-unsaturated aldehyde-induced modifications of milk proteins and polyphenol interventions in multiphase food systems\",\"authors\":\"Ting-qi Yang , Kaiyu Jiang , Juncai Tu , Yuxuan Liang , Menghui Wang , Beiwei Zhu , Wei Gong\",\"doi\":\"10.1016/j.foodhyd.2025.111962\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Lipid peroxidation remains an inevitable challenge during dairy processing and storage. The α, β-unsaturated aldehydes produced during lipid peroxidation are highly reactive with proteins, which can degrade the stability and nutritional quality of dairy products. Polyphenols are widely used as antioxidants to control degradation caused by α, β-unsaturated aldehydes. However, most studies focus on homogeneous systems, overlooking the influence of the complex interfaces inherent in dairy products on protein modification by α, β-unsaturated aldehydes and the intervention of polyphenols. Herein, we established a Hex-milk protein interfacial model system and employed clickable probes (yne-ACR) to simulate the modification of milk proteins by α, β-unsaturated aldehydes. Additionally, six polyphenols with different structures were added to intervene the modification by yne-ACR. Results demonstrated that both yne-ACR modification and the intervention of different polyphenols significantly altered the dynamic interfacial behavior and expansion rheological properties of milk proteins. However, the impact on the stability of the interface model system was minimal. Notably, casein in milk proteins predominantly adsorbed at the interface. The in-gel fluorescence imaging revealed that the presence of the interface enhanced the modification of milk proteins by yne-ACR. The intervention effects of polyphenols varied based on their structural characteristics: PA, GA, GeA, RA, and EC inhibited the modification of non-adsorbed β-lactoglobulin (β-Lg) by yne-ACR, while EGCG significantly suppressed yne-ACR modification of both interfacial and non-adsorbed proteins and notably reduced protein carbonylation. This study highlights the critical role of interface microenvironment in influencing α, β-unsaturated aldehyde-protein interactions and analyzes the intervention effects of polyphenols with varying structures in complex food systems. These findings provide a theoretical foundation for the rational use of antioxidant strategies in dairy processing.</div></div>\",\"PeriodicalId\":320,\"journal\":{\"name\":\"Food Hydrocolloids\",\"volume\":\"172 \",\"pages\":\"Article 111962\"},\"PeriodicalIF\":11.0000,\"publicationDate\":\"2025-09-16\",\"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/S0268005X25009221\",\"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/S0268005X25009221","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}
Novel insights into interfacial effects on α, β-unsaturated aldehyde-induced modifications of milk proteins and polyphenol interventions in multiphase food systems
Lipid peroxidation remains an inevitable challenge during dairy processing and storage. The α, β-unsaturated aldehydes produced during lipid peroxidation are highly reactive with proteins, which can degrade the stability and nutritional quality of dairy products. Polyphenols are widely used as antioxidants to control degradation caused by α, β-unsaturated aldehydes. However, most studies focus on homogeneous systems, overlooking the influence of the complex interfaces inherent in dairy products on protein modification by α, β-unsaturated aldehydes and the intervention of polyphenols. Herein, we established a Hex-milk protein interfacial model system and employed clickable probes (yne-ACR) to simulate the modification of milk proteins by α, β-unsaturated aldehydes. Additionally, six polyphenols with different structures were added to intervene the modification by yne-ACR. Results demonstrated that both yne-ACR modification and the intervention of different polyphenols significantly altered the dynamic interfacial behavior and expansion rheological properties of milk proteins. However, the impact on the stability of the interface model system was minimal. Notably, casein in milk proteins predominantly adsorbed at the interface. The in-gel fluorescence imaging revealed that the presence of the interface enhanced the modification of milk proteins by yne-ACR. The intervention effects of polyphenols varied based on their structural characteristics: PA, GA, GeA, RA, and EC inhibited the modification of non-adsorbed β-lactoglobulin (β-Lg) by yne-ACR, while EGCG significantly suppressed yne-ACR modification of both interfacial and non-adsorbed proteins and notably reduced protein carbonylation. This study highlights the critical role of interface microenvironment in influencing α, β-unsaturated aldehyde-protein interactions and analyzes the intervention effects of polyphenols with varying structures in complex food systems. These findings provide a theoretical foundation for the rational use of antioxidant strategies in dairy processing.
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.