Structural properties of canola protein isolate-gum Arabic Maillard conjugate in an aqueous model system

Structural properties of canola protein isolate-gum Arabic Maillard conjugate in an aqueous model... We aimed to study the effect of conjugation with gum Arabic (GA) by Maillard reaction in aqueous solution on the structural properties of Canola protein isolate (CPI). First, the grafting of GA to CPI through Maillard reaction was confirmed by examination of the Fourier transform infrared spectra. The results showed that the thermal stability of CPI was remarkably improved by mixing or conjugating with GA. The evidence of particle size distribution determined by nanoparticles tracking analysis (NTA) confirmed that glycation can reduce the thermal aggregation and also nanoparticles of conjugate appear bigger than CPI. Furthermore, the tertiary structure of protein in conjugate changed with decreasing number of aromatic side-chains exposed in heating environment. The decrease in fluorescence intensity of conjugate was related to conformational changes due to presence of GA. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Food Hydrocolloids Elsevier

Structural properties of canola protein isolate-gum Arabic Maillard conjugate in an aqueous model system

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Publisher
Elsevier
Copyright
Copyright © 2018 Elsevier Ltd
ISSN
0268-005X
eISSN
1873-7137
D.O.I.
10.1016/j.foodhyd.2018.01.001
Publisher site
See Article on Publisher Site

Abstract

We aimed to study the effect of conjugation with gum Arabic (GA) by Maillard reaction in aqueous solution on the structural properties of Canola protein isolate (CPI). First, the grafting of GA to CPI through Maillard reaction was confirmed by examination of the Fourier transform infrared spectra. The results showed that the thermal stability of CPI was remarkably improved by mixing or conjugating with GA. The evidence of particle size distribution determined by nanoparticles tracking analysis (NTA) confirmed that glycation can reduce the thermal aggregation and also nanoparticles of conjugate appear bigger than CPI. Furthermore, the tertiary structure of protein in conjugate changed with decreasing number of aromatic side-chains exposed in heating environment. The decrease in fluorescence intensity of conjugate was related to conformational changes due to presence of GA.

Journal

Food HydrocolloidsElsevier

Published: Jun 1, 2018

References

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