Formation mechanism of ovalbumin gel induced by alkali

Formation mechanism of ovalbumin gel induced by alkali In this paper, the alkali-induced gelling behavior of ovalbumin, including its microstructure characteristics, intermolecular forces, and molecular structure changes, was investigated. The results showed that ovalbumin formed a three-dimensional gel with an ordered fibrous mesh structure under alkali conditions. The active force between gel molecules was maintained by a large number of ionic bonds (∼85%), a small number of disulfide bonds (∼5%), and very few hydrophobic interactions and hydrogen bonds. SDS-PAGE analysis showed that ovalbumin formed aggregates via ionic and disulfide bonds. ANS fluorescence spectroscopy analysis showed that strong alkali caused rapid denaturation of ovalbumin molecules to expose the hydrophobic core, thus greatly increasing the surface hydrophobicity. However, the hydrophobicity decreased during the gelation stage. FTIR analysis showed that strong alkali induced the secondary-level structure of ovalbumin molecules to interconvert, and most of them existed in a relatively stable α-folding structure. Endogenous fluorescence and UV spectroscopic analyses showed that the amino acid residues of ovalbumin in the gelation stage moved towards the polar environment. It was concluded that the secondary and tertiary structures of ovalbumin changed after treatment with strong alkali and that a crystal gel formed through the action of ionic and disulfide bonds. In addition, the long-term action of strong alkali gradually decreased the gelatinous property. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Food Hydrocolloids Elsevier

Formation mechanism of ovalbumin gel induced by alkali

Loading next page...
 
/lp/elsevier/formation-mechanism-of-ovalbumin-gel-induced-by-alkali-62gNsjNvoR
Publisher
Elsevier
Copyright
Copyright © 2016 Elsevier Ltd
ISSN
0268-005X
eISSN
1873-7137
D.O.I.
10.1016/j.foodhyd.2016.04.041
Publisher site
See Article on Publisher Site

Abstract

In this paper, the alkali-induced gelling behavior of ovalbumin, including its microstructure characteristics, intermolecular forces, and molecular structure changes, was investigated. The results showed that ovalbumin formed a three-dimensional gel with an ordered fibrous mesh structure under alkali conditions. The active force between gel molecules was maintained by a large number of ionic bonds (∼85%), a small number of disulfide bonds (∼5%), and very few hydrophobic interactions and hydrogen bonds. SDS-PAGE analysis showed that ovalbumin formed aggregates via ionic and disulfide bonds. ANS fluorescence spectroscopy analysis showed that strong alkali caused rapid denaturation of ovalbumin molecules to expose the hydrophobic core, thus greatly increasing the surface hydrophobicity. However, the hydrophobicity decreased during the gelation stage. FTIR analysis showed that strong alkali induced the secondary-level structure of ovalbumin molecules to interconvert, and most of them existed in a relatively stable α-folding structure. Endogenous fluorescence and UV spectroscopic analyses showed that the amino acid residues of ovalbumin in the gelation stage moved towards the polar environment. It was concluded that the secondary and tertiary structures of ovalbumin changed after treatment with strong alkali and that a crystal gel formed through the action of ionic and disulfide bonds. In addition, the long-term action of strong alkali gradually decreased the gelatinous property.

Journal

Food HydrocolloidsElsevier

Published: Dec 1, 2016

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