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Complexation of curcumin with soy protein isolate and its implications on solubility and stability of curcumin.

Arun, Tapal and Purnima Kaul, Tiku (2012) Complexation of curcumin with soy protein isolate and its implications on solubility and stability of curcumin. Food Chemistry, 130. pp. 960-965. ISSN 0308-8146

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Abstract

Curcumin, a natural polyphenolic food colourant, suffers a low bioavailability because of its low solubility and instability in aqueous solutions. Our study demonstrates that the food derived soy protein isolate (SPI) can form a complex with the curcumin. Fluorescence spectroscopy of the SPI–curcumin complex revealed that the complex is formed through hydrophobic interactions. Moreover, curcumin molecules quench the intrinsic fluorescence of SPI upon binding. Upon complexation, curcumin showed increased water solubility. Stability studies by UV spectroscopy showed that >80% of the curcumin was stable in the SPI–curcumin complex when dissolved in water, simulated gastric and intestinal fluids for 12 h, which would provide sufficient time for intestinal absorption. SPI–curcumin complex exhibits enhanced antioxidant activity and is capable of forming foam and emulsion, indicating its possible utilisation in food product formulation. This study suggests that SPI, being an edible protein, could be used as a material to encapsulate water-insoluble bioactive compounds in functional foods.

Item Type: Article
Uncontrolled Keywords: Soyproteinisolate; Curcumin; Solubility; Stability; Complexation
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
600 Technology > 08 Food technology > 22 Legumes-Pulses > 05 Soya bean
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 24 Jan 2012 11:30
Last Modified: 09 May 2012 04:55
URI: http://ir.cftri.com/id/eprint/10574

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