Structural architecture and solubility of native and modified gliadin and glutenin proteins: non-crystalline molecular and atomic organization
(2014) In RSC Advances 4(4). p.2051-2060- Abstract
- Wheat gluten (WG) and its components, gliadin and glutenin proteins, form the largest polymers in nature, which complicates the structural architecture of these proteins. Wheat gluten, gliadin and glutenin
proteins in unmodified form showed few secondary structural features. Structural modification of these proteins using heat, pressure and the chemical chaperone glycerol resulted in a shift to organized
structure. In modified gliadin, nano-structural molecular arrangements in the form of hexagonal closed pack (HCP) assemblies with lattice parameter of (58 Å) were obvious together with development of intermolecular disulphide bonds. Modification of glutenin resulted in highly polymerized structure with proteins linked not... (More) - Wheat gluten (WG) and its components, gliadin and glutenin proteins, form the largest polymers in nature, which complicates the structural architecture of these proteins. Wheat gluten, gliadin and glutenin
proteins in unmodified form showed few secondary structural features. Structural modification of these proteins using heat, pressure and the chemical chaperone glycerol resulted in a shift to organized
structure. In modified gliadin, nano-structural molecular arrangements in the form of hexagonal closed pack (HCP) assemblies with lattice parameter of (58 Å) were obvious together with development of intermolecular disulphide bonds. Modification of glutenin resulted in highly polymerized structure with proteins linked not only by disulphide bonds, but also with other covalent and irreversible bonds, as well as the highest proportion of b-sheets. From a combination of experimental evidence and protein algorithms, we have proposed tertiary structure models of unmodified and modified gliadin and glutenin proteins. An increased understanding of gliadin and glutenin proteins structure and behavior are of utmost importance to understand the applicability of these proteins for various applications including plastics materials, foams, adhesives, films and coatings. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4178278
- author
- Rasheed, Faiza ; Newson, William R. ; Plivelic, Tomás LU ; Kuktaite, Ramune ; Hedenqvist, Mikael S. ; Gällstedt, Mikael and Johansson, Eva
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- RSC Advances
- volume
- 4
- issue
- 4
- pages
- 2051 - 2060
- publisher
- Royal Society of Chemistry
- external identifiers
-
- wos:000329033700070
- scopus:84890034091
- ISSN
- 2046-2069
- DOI
- 10.1039/c3ra45522j
- language
- English
- LU publication?
- yes
- id
- 3c67cc29-9f85-4ba8-afc0-ae8b0fb3a59a (old id 4178278)
- alternative location
- http://pubs.rsc.org/en/content/articlelanding/2013/ra/c3ra45522j#!divAbstract
- date added to LUP
- 2016-04-01 14:02:38
- date last changed
- 2022-01-27 22:33:30
@article{3c67cc29-9f85-4ba8-afc0-ae8b0fb3a59a,
abstract = {{Wheat gluten (WG) and its components, gliadin and glutenin proteins, form the largest polymers in nature, which complicates the structural architecture of these proteins. Wheat gluten, gliadin and glutenin<br/><br>
proteins in unmodified form showed few secondary structural features. Structural modification of these proteins using heat, pressure and the chemical chaperone glycerol resulted in a shift to organized<br/><br>
structure. In modified gliadin, nano-structural molecular arrangements in the form of hexagonal closed pack (HCP) assemblies with lattice parameter of (58 Å) were obvious together with development of intermolecular disulphide bonds. Modification of glutenin resulted in highly polymerized structure with proteins linked not only by disulphide bonds, but also with other covalent and irreversible bonds, as well as the highest proportion of b-sheets. From a combination of experimental evidence and protein algorithms, we have proposed tertiary structure models of unmodified and modified gliadin and glutenin proteins. An increased understanding of gliadin and glutenin proteins structure and behavior are of utmost importance to understand the applicability of these proteins for various applications including plastics materials, foams, adhesives, films and coatings.}},
author = {{Rasheed, Faiza and Newson, William R. and Plivelic, Tomás and Kuktaite, Ramune and Hedenqvist, Mikael S. and Gällstedt, Mikael and Johansson, Eva}},
issn = {{2046-2069}},
language = {{eng}},
number = {{4}},
pages = {{2051--2060}},
publisher = {{Royal Society of Chemistry}},
series = {{RSC Advances}},
title = {{Structural architecture and solubility of native and modified gliadin and glutenin proteins: non-crystalline molecular and atomic organization}},
url = {{http://dx.doi.org/10.1039/c3ra45522j}},
doi = {{10.1039/c3ra45522j}},
volume = {{4}},
year = {{2014}},
}