{"title":"乳清蛋白与赤藓糖醇之间的相互作用对蛋白质构象、界面特性和稳定性的影响","authors":"Yumeng Zhang, Juan Zhang, Junhua Shao, Mohan Li, Xiqing Yue, Aijun Xie","doi":"10.1111/1471-0307.13092","DOIUrl":null,"url":null,"abstract":"<p>This study investigated the impact of erythritol (ERY) on structural and functional properties of whey protein isolate (WPI). FTIR and CD revealed that WPI underwent structural changes, including formation of β-folds and random coils, upon interaction with 20 mg/mL ERY. SEM showed increased surface roughness of WPI, indicating enhanced protein exposure. Moreover, binding rate exceeded 85%, accompanied by increased surface hydrophobicity. Fluorescence spectroscopy indicated a red shift in fluorescence of WPI and tyrosine (Tyr) residues, altering polarity of Tyr environment due to ERY coordination. Additionally, ERY presence enhanced the functional properties of WPI, including foaming, freeze–thaw stability, rheology and antioxidant activity.</p>","PeriodicalId":13822,"journal":{"name":"International Journal of Dairy Technology","volume":null,"pages":null},"PeriodicalIF":2.5000,"publicationDate":"2024-04-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The influence of the interaction between whey protein and erythritol on protein conformation, interfacial properties and stability\",\"authors\":\"Yumeng Zhang, Juan Zhang, Junhua Shao, Mohan Li, Xiqing Yue, Aijun Xie\",\"doi\":\"10.1111/1471-0307.13092\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>This study investigated the impact of erythritol (ERY) on structural and functional properties of whey protein isolate (WPI). FTIR and CD revealed that WPI underwent structural changes, including formation of β-folds and random coils, upon interaction with 20 mg/mL ERY. SEM showed increased surface roughness of WPI, indicating enhanced protein exposure. Moreover, binding rate exceeded 85%, accompanied by increased surface hydrophobicity. Fluorescence spectroscopy indicated a red shift in fluorescence of WPI and tyrosine (Tyr) residues, altering polarity of Tyr environment due to ERY coordination. Additionally, ERY presence enhanced the functional properties of WPI, including foaming, freeze–thaw stability, rheology and antioxidant activity.</p>\",\"PeriodicalId\":13822,\"journal\":{\"name\":\"International Journal of Dairy Technology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.5000,\"publicationDate\":\"2024-04-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International Journal of Dairy Technology\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1111/1471-0307.13092\",\"RegionNum\":2,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Dairy Technology","FirstCategoryId":"97","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1111/1471-0307.13092","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
The influence of the interaction between whey protein and erythritol on protein conformation, interfacial properties and stability
This study investigated the impact of erythritol (ERY) on structural and functional properties of whey protein isolate (WPI). FTIR and CD revealed that WPI underwent structural changes, including formation of β-folds and random coils, upon interaction with 20 mg/mL ERY. SEM showed increased surface roughness of WPI, indicating enhanced protein exposure. Moreover, binding rate exceeded 85%, accompanied by increased surface hydrophobicity. Fluorescence spectroscopy indicated a red shift in fluorescence of WPI and tyrosine (Tyr) residues, altering polarity of Tyr environment due to ERY coordination. Additionally, ERY presence enhanced the functional properties of WPI, including foaming, freeze–thaw stability, rheology and antioxidant activity.
期刊介绍：
The International Journal of Dairy Technology ranks highly among the leading dairy journals published worldwide, and is the flagship of the Society. As indicated in its title, the journal is international in scope.
Published quarterly, International Journal of Dairy Technology contains original papers and review articles covering topics that are at the interface between fundamental dairy research and the practical technological challenges facing the modern dairy industry worldwide. Topics addressed span the full range of dairy technologies, the production of diverse dairy products across the world and the development of dairy ingredients for food applications.
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