耐乙醇双蛋白纳米颗粒：抑制乳铁蛋白聚集和稳定乙醇-水体系中的皮克林乳状液

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids Pub Date : 2025-05-11 DOI:10.1016/j.foodhyd.2025.111533

Yuan Wang , Jingying Xie , Yahong Wang , Wenyan Liao , Yanxiang Gao

{"title":"耐乙醇双蛋白纳米颗粒：抑制乳铁蛋白聚集和稳定乙醇-水体系中的皮克林乳状液","authors":"Yuan Wang , Jingying Xie , Yahong Wang , Wenyan Liao , Yanxiang Gao","doi":"10.1016/j.foodhyd.2025.111533","DOIUrl":null,"url":null,"abstract":"<div><div>Lactoferrin (LF) is widely recognized for its biological activities, yet its tendency to aggregate in ethanol-containing environments limits its application in alcoholic beverages. In this study, Zein nanoparticles were employed to modulate LF aggregation and enhance its stability in 15 % (v/v) ethanol-water system. The results demonstrated that Zein effectively inhibited LF aggregation and facilitated the formation of LF-Zein dual-protein nanoparticles. At an optimal mass ratio of LF to Zein (1:1), the nanoparticles exhibited the smallest diameter (110.9 ± 8.4 nm) and the highest zeta-potential (+45.8 ± 1.6 mV), indicating its improved colloidal stability. Circular dichroism (CD) spectroscopy revealed an increase in α-helix content, enhancing the thermal stability of LF. Isothermal titration calorimetry (ITC) and molecular docking analyses confirmed that hydrophobic interactions between LF and Zein played a dominant role in the nanoparticle formation, complemented by hydrogen bonding and van der Waals forces. Furthermore, the dual-protein nanoparticles exhibited strong interfacial activity, significantly reducing interfacial tension and stabilizing Pickering emulsions, as evidenced by lower Turbiscan stability index (TSI) values. These findings suggest that the construction of LF-Zein dual-protein nanoparticles provides a promising strategy for inhibiting LF aggregation in ethanol-rich environments and facilitates its application in alcoholic emulsions and functional beverages.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"168 ","pages":"Article 111533"},"PeriodicalIF":11.0000,"publicationDate":"2025-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Ethanol-tolerant dual-protein nanoparticles: Inhibiting lactoferrin aggregation and stabilizing Pickering emulsions in ethanol-water system\",\"authors\":\"Yuan Wang , Jingying Xie , Yahong Wang , Wenyan Liao , Yanxiang Gao\",\"doi\":\"10.1016/j.foodhyd.2025.111533\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Lactoferrin (LF) is widely recognized for its biological activities, yet its tendency to aggregate in ethanol-containing environments limits its application in alcoholic beverages. In this study, Zein nanoparticles were employed to modulate LF aggregation and enhance its stability in 15 % (v/v) ethanol-water system. The results demonstrated that Zein effectively inhibited LF aggregation and facilitated the formation of LF-Zein dual-protein nanoparticles. At an optimal mass ratio of LF to Zein (1:1), the nanoparticles exhibited the smallest diameter (110.9 ± 8.4 nm) and the highest zeta-potential (+45.8 ± 1.6 mV), indicating its improved colloidal stability. Circular dichroism (CD) spectroscopy revealed an increase in α-helix content, enhancing the thermal stability of LF. Isothermal titration calorimetry (ITC) and molecular docking analyses confirmed that hydrophobic interactions between LF and Zein played a dominant role in the nanoparticle formation, complemented by hydrogen bonding and van der Waals forces. Furthermore, the dual-protein nanoparticles exhibited strong interfacial activity, significantly reducing interfacial tension and stabilizing Pickering emulsions, as evidenced by lower Turbiscan stability index (TSI) values. These findings suggest that the construction of LF-Zein dual-protein nanoparticles provides a promising strategy for inhibiting LF aggregation in ethanol-rich environments and facilitates its application in alcoholic emulsions and functional beverages.</div></div>\",\"PeriodicalId\":320,\"journal\":{\"name\":\"Food Hydrocolloids\",\"volume\":\"168 \",\"pages\":\"Article 111533\"},\"PeriodicalIF\":11.0000,\"publicationDate\":\"2025-05-11\",\"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/S0268005X2500493X\",\"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/S0268005X2500493X","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

乳铁蛋白（LF）因其生物活性而得到广泛认可，但其在含乙醇环境中的聚集性限制了其在酒精饮料中的应用。在本研究中，利用玉米蛋白纳米颗粒调节LF的聚集，提高其在15% （v/v）乙醇-水体系中的稳定性。结果表明，玉米蛋白可有效抑制LF聚集，促进LF-Zein双蛋白纳米颗粒的形成。当蛋白与玉米蛋白的质量比为1:1时，纳米颗粒直径最小（110.9±8.4 nm）， ζ电位最高（+45.8±1.6 mV），胶体稳定性得到改善。圆二色性（CD）光谱显示α-螺旋含量增加，增强了LF的热稳定性。等温滴定量热法（ITC）和分子对接分析证实，LF和Zein之间的疏水相互作用在纳米颗粒的形成中起主导作用，氢键和范德华力也起补充作用。此外，双蛋白纳米颗粒表现出很强的界面活性，可以显著降低界面张力，稳定皮克林乳状液，这一点可以从较低的Turbiscan稳定性指数（TSI）中得到证明。这些发现表明，构建LF- zein双蛋白纳米颗粒为抑制LF在富含乙醇环境中的聚集提供了一种有前途的策略，并促进了其在酒精乳液和功能饮料中的应用。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文本刊更多论文

Ethanol-tolerant dual-protein nanoparticles: Inhibiting lactoferrin aggregation and stabilizing Pickering emulsions in ethanol-water system

Lactoferrin (LF) is widely recognized for its biological activities, yet its tendency to aggregate in ethanol-containing environments limits its application in alcoholic beverages. In this study, Zein nanoparticles were employed to modulate LF aggregation and enhance its stability in 15 % (v/v) ethanol-water system. The results demonstrated that Zein effectively inhibited LF aggregation and facilitated the formation of LF-Zein dual-protein nanoparticles. At an optimal mass ratio of LF to Zein (1:1), the nanoparticles exhibited the smallest diameter (110.9 ± 8.4 nm) and the highest zeta-potential (+45.8 ± 1.6 mV), indicating its improved colloidal stability. Circular dichroism (CD) spectroscopy revealed an increase in α-helix content, enhancing the thermal stability of LF. Isothermal titration calorimetry (ITC) and molecular docking analyses confirmed that hydrophobic interactions between LF and Zein played a dominant role in the nanoparticle formation, complemented by hydrogen bonding and van der Waals forces. Furthermore, the dual-protein nanoparticles exhibited strong interfacial activity, significantly reducing interfacial tension and stabilizing Pickering emulsions, as evidenced by lower Turbiscan stability index (TSI) values. These findings suggest that the construction of LF-Zein dual-protein nanoparticles provides a promising strategy for inhibiting LF aggregation in ethanol-rich environments and facilitates its application in alcoholic emulsions and functional beverages.

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

Food Hydrocolloids 工程技术-食品科技

CiteScore

19.90

自引率

14.00%

发文量

871

审稿时长

37 days

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.