Effect of alkaline extraction on the structure of the protein of quinoa (Chenopodium quinoa Willd.) and its influence on film formation
Version of Record online: 3 DEC 2012
© 2012 The Authors. International Journal of Food Science and Technology © 2012 Institute of Food Science and Technology
International Journal of Food Science & Technology
Volume 48, Issue 4, pages 843–849, April 2013
How to Cite
Valenzuela, C., Abugoch, L., Tapia, C. and Gamboa, A. (2013), Effect of alkaline extraction on the structure of the protein of quinoa (Chenopodium quinoa Willd.) and its influence on film formation. International Journal of Food Science & Technology, 48: 843–849. doi: 10.1111/ijfs.12035
- Issue online: 11 MAR 2013
- Version of Record online: 3 DEC 2012
- Manuscript Accepted: 23 SEP 2012
- Manuscript Received: 2 APR 2012
Figure S1. SDS-PAGE profiles of aqueous extract of quinoa protein (PE) treated at pH 8–12. No reducing conditions (left lanes);M is the protein standard; and with 2-ME (right lanes). Gl, indicate the band of globuline. AS corresponds to acidic subunit, and BS to basic subunit.
Figure S2. Size-exclusion chromatography coupled with evaporative light scattering of aqueous extract of quinoa protein (PE) treated between pH 8 to 12. A1, A2 correspond to protein aggregates, and F1, F2 and F3 indicate the protein fractions.
Figure S3. Fluorescence emission spectrum of aqueous extracts of quinoa protein (PE) treated at pH 8–12.
Figure S4. Fourier transform infrared spectroscopy spectra of quinoa protein film at pH 12.
Figure S5 Scanning electron micrographs (SEM) of surface quinoa protein film at pH 12. (a) 5009 (b) 20009 (c) 50009 and (d) 80009.
|ijfs12035-sup-0002-TableS1.doc||Word document||41K||Table S1. Free (SHf), exposed (SHe), total (SHt) sulphydryl groups and disulphide bonds (SS) of aqueous extract of quinoa protein (PE) treated between pH 8–12.|
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