Ruiling Li , Chao Ma , Ningzhe Wang , Jing Wang , Xin Yang
{"title":"探索超声改善蛋白基乳液凝胶理化性质的潜力:分别对乳液(乳化前、乳化后)和底物溶液进行超声处理","authors":"Ruiling Li , Chao Ma , Ningzhe Wang , Jing Wang , Xin Yang","doi":"10.1016/j.foodhyd.2025.111492","DOIUrl":null,"url":null,"abstract":"<div><div>Emulsion gels prepared from proteins had excellent texture properties, rheological properties and storage stability. Unlike improved the material properties of protein-based emulsion gels by ultrasonic treatment at different frequencies with different durations. In this study, we divided the protein-based emulsion gel into two components: emulsion and substrate solution. Three types of ultrasound treatment were used for each of these two components of the emulsion gel: a. Proteins in the emulsion were ultrasonicated before emulsifying the oil droplets; b. Proteins in the emulsion were ultrasonicated after emulsifying the oil droplets; c. Proteins in the substrate solution were ultrasonicated. The emulsions and substrate solutions formed by these three ultrasound methods were mixed with the non-ultrasonicated substrate solution and emulsion solution, respectively, and heated to form three emulsion gels, Pre-E, Post-E, and Ss. Pre-E had high hardness and water holding capacity, uniform dispersion of oil droplets, compact and dense network structure, high surface hydrophobicity and amide A peak intensity, and low free sulfhydryl content. This was because the treatment method of ultrasonication before emulsification promoted the diffusion of unfolded protein molecules on the interface and adsorbed on the surface of oil droplets to form an interface film, preventing droplet coalescence. In addition, this also promoted the uniform dispersion of these unfolded proteins in the whole system, and promoted the formation of a dense network structure between proteins by forming disulfide bonds, hydrophobic interactions, and hydrogen bond. This study explored the new potential of ultrasonic modification of the physicochemical property of protein-based emulsion gels.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"168 ","pages":"Article 111492"},"PeriodicalIF":11.0000,"publicationDate":"2025-04-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Exploring the potential of ultrasound to improve the physicochemical properties of protein-based emulsion gels: by ultrasonically treating emulsion (pre-emulsification, post-emulsification) and substrate solution respectively\",\"authors\":\"Ruiling Li , Chao Ma , Ningzhe Wang , Jing Wang , Xin Yang\",\"doi\":\"10.1016/j.foodhyd.2025.111492\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Emulsion gels prepared from proteins had excellent texture properties, rheological properties and storage stability. Unlike improved the material properties of protein-based emulsion gels by ultrasonic treatment at different frequencies with different durations. In this study, we divided the protein-based emulsion gel into two components: emulsion and substrate solution. Three types of ultrasound treatment were used for each of these two components of the emulsion gel: a. Proteins in the emulsion were ultrasonicated before emulsifying the oil droplets; b. Proteins in the emulsion were ultrasonicated after emulsifying the oil droplets; c. Proteins in the substrate solution were ultrasonicated. The emulsions and substrate solutions formed by these three ultrasound methods were mixed with the non-ultrasonicated substrate solution and emulsion solution, respectively, and heated to form three emulsion gels, Pre-E, Post-E, and Ss. Pre-E had high hardness and water holding capacity, uniform dispersion of oil droplets, compact and dense network structure, high surface hydrophobicity and amide A peak intensity, and low free sulfhydryl content. This was because the treatment method of ultrasonication before emulsification promoted the diffusion of unfolded protein molecules on the interface and adsorbed on the surface of oil droplets to form an interface film, preventing droplet coalescence. In addition, this also promoted the uniform dispersion of these unfolded proteins in the whole system, and promoted the formation of a dense network structure between proteins by forming disulfide bonds, hydrophobic interactions, and hydrogen bond. This study explored the new potential of ultrasonic modification of the physicochemical property of protein-based emulsion gels.</div></div>\",\"PeriodicalId\":320,\"journal\":{\"name\":\"Food Hydrocolloids\",\"volume\":\"168 \",\"pages\":\"Article 111492\"},\"PeriodicalIF\":11.0000,\"publicationDate\":\"2025-04-25\",\"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/S0268005X25004527\",\"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/S0268005X25004527","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 potential of ultrasound to improve the physicochemical properties of protein-based emulsion gels: by ultrasonically treating emulsion (pre-emulsification, post-emulsification) and substrate solution respectively
Emulsion gels prepared from proteins had excellent texture properties, rheological properties and storage stability. Unlike improved the material properties of protein-based emulsion gels by ultrasonic treatment at different frequencies with different durations. In this study, we divided the protein-based emulsion gel into two components: emulsion and substrate solution. Three types of ultrasound treatment were used for each of these two components of the emulsion gel: a. Proteins in the emulsion were ultrasonicated before emulsifying the oil droplets; b. Proteins in the emulsion were ultrasonicated after emulsifying the oil droplets; c. Proteins in the substrate solution were ultrasonicated. The emulsions and substrate solutions formed by these three ultrasound methods were mixed with the non-ultrasonicated substrate solution and emulsion solution, respectively, and heated to form three emulsion gels, Pre-E, Post-E, and Ss. Pre-E had high hardness and water holding capacity, uniform dispersion of oil droplets, compact and dense network structure, high surface hydrophobicity and amide A peak intensity, and low free sulfhydryl content. This was because the treatment method of ultrasonication before emulsification promoted the diffusion of unfolded protein molecules on the interface and adsorbed on the surface of oil droplets to form an interface film, preventing droplet coalescence. In addition, this also promoted the uniform dispersion of these unfolded proteins in the whole system, and promoted the formation of a dense network structure between proteins by forming disulfide bonds, hydrophobic interactions, and hydrogen bond. This study explored the new potential of ultrasonic modification of the physicochemical property of protein-based emulsion gels.
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.