Nanocomplexation between curcumin and soy protein isolate: influence on curcumin stability/bioaccessibility and in vitro protein digestibility
Autor: | Bian-Sheng Li, Fei-Ping Chen, Chuan-He Tang |
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Rok vydání: | 2015 |
Předmět: |
Chromatography
Curcumin Hot Temperature Chemistry Hydrolysis Biological Availability Capsules General Chemistry Protein aggregation In vitro chemistry.chemical_compound Drug Stability Solubility Protein digestibility Soybean Proteins Nanoparticles Digestion Particle Size General Agricultural and Biological Sciences Soy protein Hydrophobic and Hydrophilic Interactions Nutritive Value Peptide Hydrolases |
Zdroj: | Journal of agricultural and food chemistry. 63(13) |
ISSN: | 1520-5118 |
Popis: | The complexation of nanoparticles in unheated and heated (at 75-95°) soy protein isolate (SPI) with curcumin and the effects on curcumin stability/bioaccessibility and in vitro protein digestibility were investigated. The nanoparticles did not display noticeable changes in size and morphology upon nanocomplexation with curcumin, except their surface hydrophobicity. The encapsulation efficiency of curcumin progressively decreased with increasing initial curcumin concentration in the dispersion, while the load amount linearly increased. The solubility of curcumin in water was enhanced by the complexation above 98000-fold (vs free curcumin in water). The formation of the nanocomplexes considerably improved the storage stability of curcumin. In vitro simulated digestion experiments indicated that the complexation also improved the bioaccessibility of curcumin; the bioaccessibility was greatly impaired by hydrolysis-induced protein aggregation. Addtionally, the nanocomplexation significantly improved the in vitro protein digestibility of both unheated and heated SPI. |
Databáze: | OpenAIRE |
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