食品科学 ›› 2020, Vol. 41 ›› Issue (14): 1-8.doi: 10.7506/spkx1002-6630-20190526-314

• 食品化学 •    下一篇

酸热诱导大豆分离蛋白纳米颗粒形成及其荷载姜黄素的特性

袁 丹,赵谋明,张思锐,黄 燚,周非白   

  1. (华南理工大学食品科学与工程学院,广东 广州 510640)
  • 出版日期:2020-07-25 发布日期:2020-07-29
  • 基金资助:
    国家自然科学基金青年科学基金项目(31701539)

Heat-Induced Formation of Soy Protein Nanoparticles at Acidic pH for Encapsulation of Curcumin

YUAN Dan, ZHAO Mouming, ZHANG Sirui, HUANG Yi, ZHOU Feibai   

  1. (College of Food Science and Technology, South China University of Technology, Guangzhou 510640, China)
  • Online:2020-07-25 Published:2020-07-29

摘要: 以大豆分离蛋白(soy protein isolate,SPI)为原料,在特定pH值条件下(pH 7.0、5.9)静态加热处理(95 ℃、30 min)诱导SPI自组装形成纳米颗粒,分别记作HSPI及HSPI(pH 5.9)。进一步以姜黄素为模型疏水性活性物质,较系统地比较均质及超声处理对不同结构的蛋白颗粒荷载姜黄素的影响。荧光光谱结果表明,SPI、HSPI和HSPI(pH 5.9)均可与姜黄素发生疏水相互作用,使蛋白发生荧光猝灭并提高姜黄素的水分散性。热处理可显著提高蛋白颗粒的表面疏水性,其中HSPI(pH 5.9)的粒径分布更均一(多相分散系数<0.2),且较SPI与姜黄素有更高的结合力。通过均质或超声处理,SPI、HSPI和HSPI(pH 5.9)可进一步通过疏水驱动作用荷载姜黄素形成富载姜黄素的纳米颗粒。与SPI及HSPI相比,HSPI(pH 5.9)的核-壳结构有利于蛋白与姜黄素在超声过程中发生共组装,形成形态均一且性质稳定的纳米颗粒,显著提高了姜黄素的水溶性及贮藏稳定性。

关键词: 大豆分离蛋白, 纳米颗粒, 姜黄素, 酸热处理, 荷载

Abstract: In the present study, soy protein isolate (SPI) was subjected to static heat treatment (95 ℃ for 30 min) under specific pH conditions (pH 7.0 and 5.9) to form nanoparticles through self-assembly, designated as HSPI and HSPI (pH 5.9), respectively. The influence of homogenization and sonication was comparatively investigated on the encapsulation of curcumin as a hydrophobic active ingredient into protein nanoparticles. Results from fluorescence spectroscopy showed that hydrophobic interactions between SPI, HSPI and HSPI (pH 5.9) and curcumin caused fluorescence quenching of the protein and improved the water dispersibility of curcumin. Herein, heat treatment increased the protein surface hydrophobicity and particularly promoted the formation of particles with uniformed size distribution (PDI < 0.2) at pH 5.9, noticeably enhancing the protein-curcumin interactions. Homogenization and sonication promoted the encapsulation of curcumin into SPI, HSPI and HSPI (pH 5.9) upon driven by hydrophobic forces, and the effect of the latter was more pronounced. Moreover, when compared with SPI and HSPI, the core-shell structure of HSPI (pH 5.9) facilitated its co-assembly with curcumin during sonication, forming stable nanoparticles with uniformed size distribution, which significantly improved the water solubility and storage stability of curcumin.

Key words: soy protein isolate, nanoparticle, curcumin, heat treatment at acidic pH, encapsulation

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