Yanyan Wu , Yamei Wu , Yongqiang Zhao , Huan Xiang , Zhiming Hao , Qing Wang , Yueqi Wang
{"title":"燕麦β-葡聚糖增强了肌纤维蛋白乳的稳定性和流变特性:对结构和界面相互作用的见解","authors":"Yanyan Wu , Yamei Wu , Yongqiang Zhao , Huan Xiang , Zhiming Hao , Qing Wang , Yueqi Wang","doi":"10.1016/j.foodchem.2025.143426","DOIUrl":null,"url":null,"abstract":"<div><div>The effect of oat β-glucan (OG) on the structure, interfacial behavior and emulsion rheological properties of sea bass myofibrillar protein (MP) was investigated. Fourier transform infrared spectroscopy demonstrated that adding OG decreased the α-helix content in MP from 27% to 22% and increased the β-sheet content, suggesting that OG facilitated MP unfolding. When the OG content was 1.2%, the interfacial tension decreased by approximately 20%, and the diffusion rate increased by approximately 1.5-fold. These changes augmented the physical stability of emulsions. Rheological analysis showed that 3% OG promoted the energy storage modulus (G') of the emulsion. These changes enhanced MP adsorption and rearrangement at the oil-water interface, which enhanced viscoelasticity in the interfacial film and further increased the emulsion stability. These findings augment the understanding of protein-polysaccharide interactions and provide guidance for improving protein emulsion stability.</div></div>","PeriodicalId":318,"journal":{"name":"Food Chemistry","volume":"476 ","pages":"Article 143426"},"PeriodicalIF":9.8000,"publicationDate":"2025-02-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Enhanced stability and rheological properties of myofibrillar proteins emulsions conferred by oat β-glucan: Insights into structural and interfacial interactions\",\"authors\":\"Yanyan Wu , Yamei Wu , Yongqiang Zhao , Huan Xiang , Zhiming Hao , Qing Wang , Yueqi Wang\",\"doi\":\"10.1016/j.foodchem.2025.143426\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>The effect of oat β-glucan (OG) on the structure, interfacial behavior and emulsion rheological properties of sea bass myofibrillar protein (MP) was investigated. Fourier transform infrared spectroscopy demonstrated that adding OG decreased the α-helix content in MP from 27% to 22% and increased the β-sheet content, suggesting that OG facilitated MP unfolding. When the OG content was 1.2%, the interfacial tension decreased by approximately 20%, and the diffusion rate increased by approximately 1.5-fold. These changes augmented the physical stability of emulsions. Rheological analysis showed that 3% OG promoted the energy storage modulus (G') of the emulsion. These changes enhanced MP adsorption and rearrangement at the oil-water interface, which enhanced viscoelasticity in the interfacial film and further increased the emulsion stability. These findings augment the understanding of protein-polysaccharide interactions and provide guidance for improving protein emulsion stability.</div></div>\",\"PeriodicalId\":318,\"journal\":{\"name\":\"Food Chemistry\",\"volume\":\"476 \",\"pages\":\"Article 143426\"},\"PeriodicalIF\":9.8000,\"publicationDate\":\"2025-02-16\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Chemistry\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0308814625006776\",\"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 Chemistry","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0308814625006776","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}
引用次数: 0
摘要
研究了燕麦β-葡聚糖(OG)对海鲈肌纤维蛋白(MP)的结构、界面行为和乳液流变特性的影响。傅立叶变换红外光谱显示,加入 OG 后,MP 中的α-螺旋含量从 27% 降至 22%,而β-片状含量则有所增加,这表明 OG 有助于 MP 的展开。当 OG 含量为 1.2% 时,界面张力降低了约 20%,扩散速率增加了约 1.5 倍。这些变化增强了乳液的物理稳定性。流变分析表明,3% 的 OG 提高了乳液的储能模量(G')。这些变化增强了 MP 在油水界面的吸附和重排,从而增强了界面薄膜的粘弹性,进一步提高了乳液的稳定性。这些发现加深了人们对蛋白质与多糖相互作用的理解,并为提高蛋白质乳液稳定性提供了指导。
Enhanced stability and rheological properties of myofibrillar proteins emulsions conferred by oat β-glucan: Insights into structural and interfacial interactions
The effect of oat β-glucan (OG) on the structure, interfacial behavior and emulsion rheological properties of sea bass myofibrillar protein (MP) was investigated. Fourier transform infrared spectroscopy demonstrated that adding OG decreased the α-helix content in MP from 27% to 22% and increased the β-sheet content, suggesting that OG facilitated MP unfolding. When the OG content was 1.2%, the interfacial tension decreased by approximately 20%, and the diffusion rate increased by approximately 1.5-fold. These changes augmented the physical stability of emulsions. Rheological analysis showed that 3% OG promoted the energy storage modulus (G') of the emulsion. These changes enhanced MP adsorption and rearrangement at the oil-water interface, which enhanced viscoelasticity in the interfacial film and further increased the emulsion stability. These findings augment the understanding of protein-polysaccharide interactions and provide guidance for improving protein emulsion stability.
期刊介绍:
Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.