Yu Xiao , Min-hsiung Pan , Yi-shiou Chiou , Zhenshun Li , Shudong Wei , Xiaoli Yin , Baomiao Ding
{"title":"纳米脂质体-大豆分离蛋白相互作用对大豆分离蛋白乳化特性影响的机理研究","authors":"Yu Xiao , Min-hsiung Pan , Yi-shiou Chiou , Zhenshun Li , Shudong Wei , Xiaoli Yin , Baomiao Ding","doi":"10.1016/j.foostr.2023.100357","DOIUrl":null,"url":null,"abstract":"<div><p><span>The purpose of this study was to reveal the mechanism of the improvement of SPI emulsifying properties after complexation with NL. The binding between NL and SPI led to a static fluorescence quenching of SPI and the significant change of SPI FTIR spectra. It indicated that the advanced structure of SPI after interaction with NL was altered appreciably. Moreover, it was observed that the free sulfhydryl content, contact angle, particle size, zeta potential, and surface hydrophobicity of SPI after complexation increased, and the interfacial tension reduced. Hydrophobic forces and hydrogen bonds played a vital part in the interaction between NL and SPI. Furthermore, the emulsifying properties of SPI were significantly improved after complexation with NL. Emulsifying activity index (EAI) and emulsifying stability index (ESI) of SPI increased from 50.52 to 104.28 m</span><sup>2</sup>/g and from 17.30 to 25.10 min with the NL-to-SPI mass ratio increasing from 0:1–1:1, respectively. Meanwhile, the emulsifying properties of NL-SPI (the NL-to-SPI mass ratio at 1:1) were also influenced by environmental factors (pH, temperature, and ionic strength). The improvement of the emulsifying properties of SPI after interaction with NL derived from the alteration of advanced structure and surface characteristics of NL-SPI complexes.</p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"39 ","pages":"Article 100357"},"PeriodicalIF":5.6000,"publicationDate":"2023-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Mechanistic understanding of the effects of nanoliposome-soybean protein isolate interactions on soybean protein isolate emulsifying properties\",\"authors\":\"Yu Xiao , Min-hsiung Pan , Yi-shiou Chiou , Zhenshun Li , Shudong Wei , Xiaoli Yin , Baomiao Ding\",\"doi\":\"10.1016/j.foostr.2023.100357\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p><span>The purpose of this study was to reveal the mechanism of the improvement of SPI emulsifying properties after complexation with NL. The binding between NL and SPI led to a static fluorescence quenching of SPI and the significant change of SPI FTIR spectra. It indicated that the advanced structure of SPI after interaction with NL was altered appreciably. Moreover, it was observed that the free sulfhydryl content, contact angle, particle size, zeta potential, and surface hydrophobicity of SPI after complexation increased, and the interfacial tension reduced. Hydrophobic forces and hydrogen bonds played a vital part in the interaction between NL and SPI. Furthermore, the emulsifying properties of SPI were significantly improved after complexation with NL. Emulsifying activity index (EAI) and emulsifying stability index (ESI) of SPI increased from 50.52 to 104.28 m</span><sup>2</sup>/g and from 17.30 to 25.10 min with the NL-to-SPI mass ratio increasing from 0:1–1:1, respectively. Meanwhile, the emulsifying properties of NL-SPI (the NL-to-SPI mass ratio at 1:1) were also influenced by environmental factors (pH, temperature, and ionic strength). The improvement of the emulsifying properties of SPI after interaction with NL derived from the alteration of advanced structure and surface characteristics of NL-SPI complexes.</p></div>\",\"PeriodicalId\":48640,\"journal\":{\"name\":\"Food Structure-Netherlands\",\"volume\":\"39 \",\"pages\":\"Article 100357\"},\"PeriodicalIF\":5.6000,\"publicationDate\":\"2023-11-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Structure-Netherlands\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2213329123000503\",\"RegionNum\":3,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Structure-Netherlands","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2213329123000503","RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Mechanistic understanding of the effects of nanoliposome-soybean protein isolate interactions on soybean protein isolate emulsifying properties
The purpose of this study was to reveal the mechanism of the improvement of SPI emulsifying properties after complexation with NL. The binding between NL and SPI led to a static fluorescence quenching of SPI and the significant change of SPI FTIR spectra. It indicated that the advanced structure of SPI after interaction with NL was altered appreciably. Moreover, it was observed that the free sulfhydryl content, contact angle, particle size, zeta potential, and surface hydrophobicity of SPI after complexation increased, and the interfacial tension reduced. Hydrophobic forces and hydrogen bonds played a vital part in the interaction between NL and SPI. Furthermore, the emulsifying properties of SPI were significantly improved after complexation with NL. Emulsifying activity index (EAI) and emulsifying stability index (ESI) of SPI increased from 50.52 to 104.28 m2/g and from 17.30 to 25.10 min with the NL-to-SPI mass ratio increasing from 0:1–1:1, respectively. Meanwhile, the emulsifying properties of NL-SPI (the NL-to-SPI mass ratio at 1:1) were also influenced by environmental factors (pH, temperature, and ionic strength). The improvement of the emulsifying properties of SPI after interaction with NL derived from the alteration of advanced structure and surface characteristics of NL-SPI complexes.
期刊介绍：
Food Structure is the premier international forum devoted to the publication of high-quality original research on food structure. The focus of this journal is on food structure in the context of its relationship with molecular composition, processing and macroscopic properties (e.g., shelf stability, sensory properties, etc.). Manuscripts that only report qualitative findings and micrographs and that lack sound hypothesis-driven, quantitative structure-function research are not accepted. Significance of the research findings for the food science community and/or industry must also be highlighted.
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