期刊
FOOD CHEMISTRY
卷 133, 期 2, 页码 390-399出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2012.01.049
关键词
SPI; Nanoparticles; Protein conformation changes; Nanoparticle formation mechanism; In vitro study
资金
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- China Scholarship Council
Soy protein isolate (SPI) nanoparticles (28-179 nm) were prepared by employing a cold gelation method with a slight modification. The obtained nanoparticles exhibited uniform size distribution and spherical shape with a unique honeycomb-like core structure. Nanoparticle characteristics including size, surface charge and hydrophobicity could be adjustable by changing calcium concentration and environmental pH. Generally, higher calcium concentration and lower pH led to formation of nanoparticles with larger size, lower surface charge and hydrophobicity. Both protein conformation and nanoparticle dissociation studies indicated that calcium likely shielded negative charges on the SPI polypeptide chains, and functioned as a salt-bridge to permit polypeptide chains to approach one another. In this process, calcium favoured the development of beta-sheet structures to form SPI aggregates stabilised by hydrogen bonding. These aggregates were then associated to build SPI nano-networks through hydrophobic interactions. In vitro study indicated that the SPI nanoparticles were non-toxic and mainly located in the cytoplasm when uptaken into Caco-2 cells. (C) 2012 Elsevier Ltd. All rights reserved.
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