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

Loading next page...
 
/lp/elsevier/structural-properties-of-canola-protein-isolate-gum-arabic-maillard-cLScSldsf0
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

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 12 million articles from more than
10,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Unlimited reading

Read as many articles as you need. Full articles with original layout, charts and figures. Read online, from anywhere.

Stay up to date

Keep up with your field with Personalized Recommendations and Follow Journals to get automatic updates.

Organize your research

It’s easy to organize your research with our built-in tools.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

Monthly Plan

  • Read unlimited articles
  • Personalized recommendations
  • No expiration
  • Print 20 pages per month
  • 20% off on PDF purchases
  • Organize your research
  • Get updates on your journals and topic searches

$49/month

Start Free Trial

14-day Free Trial

Best Deal — 39% off

Annual Plan

  • All the features of the Professional Plan, but for 39% off!
  • Billed annually
  • No expiration
  • For the normal price of 10 articles elsewhere, you get one full year of unlimited access to articles.

$588

$360/year

billed annually
Start Free Trial

14-day Free Trial