华南理工大学学报(自然科学版) ›› 2017, Vol. 45 ›› Issue (3): 138-145.doi: 10.3969/j.issn.1000-565X.2017.03.020

• 食品科学与技术 • 上一篇    下一篇

载荷槲皮素的酪蛋白纳米粒子输送载体的构建

游丽君1 刘敏1,2林恋竹1,2赵谋明1,2†   

  1. 1. 华南理工大学 食品科学与工程学院,广东 广州 510640;2. 广东省食品绿色加工与营养调控工程技术研究中心,广东 广州 511400
  • 收稿日期:2016-03-28 修回日期:2016-10-30 出版日期:2017-03-25 发布日期:2017-02-02
  • 通信作者: 赵谋明( 1964-) ,男,博士,教授,主要从事食品生物技术研究. E-mail:femmzhao@scut.edu.cn
  • 作者简介:游丽君( 1982-) ,女,博士,副研究员,主要从事食品营养与健康研究. E-mail: feyoulijun@ scut. edu. cn
  • 基金资助:

    国家自然科学基金资助项目( 31501424)

Construction of Casein Nanoparticles for Quercetin Delivery System

YOU Li-jun1 LIU Min1,2 LIN Lian-zhu1,2 ZHAO Mou-ming1,2   

  1. 1.School of Food Science and Engineering,South China University of Technology,Guangzhou 510640,Guangdong,China; 2.Guangdong Food Green Processing and Nutrition Regulation Technologies Research Center,Guangzhou 511400,Guangdong,China
  • Received:2016-03-28 Revised:2016-10-30 Online:2017-03-25 Published:2017-02-02
  • Contact: 赵谋明( 1964-) ,男,博士,教授,主要从事食品生物技术研究. E-mail:femmzhao@scut.edu.cn
  • About author:游丽君( 1982-) ,女,博士,副研究员,主要从事食品营养与健康研究. E-mail: feyoulijun@ scut. edu. cn
  • Supported by:

    Supported by the National Natural Science Foundation of China( 31501424)

摘要: 利用酸诱导法和热诱导法制备酪蛋白自组装纳米粒子,并构建了载荷槲皮素的酪蛋白纳米粒子输送载体,分别采用荧光光谱法、动态光散射法研究了酪蛋白纳米粒子与槲皮素的相互作用机制以及酪蛋白纳米粒子与槲皮素相互作用对酪蛋白结构、自组装特性的影响. 实验结果表明: 槲皮素可以猝灭酪蛋白内源荧光; pH5. 5、热处理所制备的酪蛋白粒子与槲皮素的结合能力最强; 酪蛋白纳米粒子- 槲皮素复合物的形成过程是自发和放热的过程,主要作用力来自氢键; 酪蛋白纳米粒子与槲皮素的相互作用对酪蛋白的自组装特性没有显著影响; 载荷槲皮素的酪蛋白纳米粒子在储藏30 天内保持良好的稳定性;30 天时,pH 5. 5、热处理所制备的酪蛋白纳米粒子对槲皮素的保留率达75. 38%.

关键词: 酪蛋白, 槲皮素, 荧光光谱, 纳米粒子

Abstract:

Self-assembled casein nanoparticleswere prepares via acid induction and thermal induction,and aquercetin delivery system was constructed.Then,the interaction mechanism and the effect of quercetin on casein conformation were investigated by means of fluorescence spectroscopy and dynamic light scattering.The results indicate that ( 1) quercetin can quench the intrinsic fluorescence of casein; ( 2) casein nanoparticles at pH5. 5 after heat treatment possesses the strongest binding with quercetin; ( 3) the interaction between quercetin and casein is a spontaneous and exothermal process,and the main force in this process is hydrogen bonding; ( 4) the interaction between quercetin and casein nanoparticles has no great effect on the self-assembly characteristics of casein; ( 5) quercetin after a 30-day storage keeps stable; and ( 6) casein nanoparticles after a heat treatment at pH5. 5 is of the highest retention rate up to 75. 38%.

Key words: casein, quercetin, fluorescence spectrum, nanoparticle