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Aggregation of gluten proteins - from wheat seed biology to hydrogels : scientific modelling based primarily on Monte-Carlo and HPLC methods

Markgren, Joel (2022). Aggregation of gluten proteins - from wheat seed biology to hydrogels : scientific modelling based primarily on Monte-Carlo and HPLC methods. Diss. (sammanfattning/summary) Sveriges lantbruksuniv., Acta Universitatis Agriculturae Sueciae, 1652-6880
ISBN 978-91-7760-895-0
eISBN 978-91-7760-896-7
[Doctoral thesis]

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Abstract

Gluten proteins are intrinsically disordered proteins that form extensive aggregated networks in wheat seeds, where they are stored as a nutrient source for the embryo. A modelling approach involving computational biology with Monte-Carlo algorithms and wet laboratory studies, including HPLC analysis, was applied to unravel the aggregational and hydrogelforming properties of the gluten proteins. Two of the gluten proteins, “αgliadin” and “low molecular weight glutenin subunits” (LMW-GS) were found to have similar size, folding of disordered, rigid and compact structures, elliptical shape and secondary structures of random coils and turns. Both proteins also share an evolutionarily conserved motif resulting in internal disulphide bonds, which were shown to be established through hydrophobic interactions, together with the inherent order of cysteines. In laboratory conditions and simulations, it was found that gliadins formed oligomers by hydrophobic interactions and cross-links by disulphide and lanthionine bonds at peptide sections in the C-terminal part of the protein. At the N-terminal part, the protein formed oligomers by liquid-liquid phase separation, polyproline II structures and β-sheets. Heat and alkaline treatment was shown to favour cross-linking by lanthionine, lysinoalanine and disulphide bonds among gliadins and increase their ability to absorb liquid. Thus the modelling approach successfully characterised the gluten proteins α-gliadin and LMW-GS, the mechanisms by which they form internal and external cross-links, how they merge into oligomers and how to increase their liquid absorption.

Authors/Creators:Markgren, Joel
Title:Aggregation of gluten proteins - from wheat seed biology to hydrogels : scientific modelling based primarily on Monte-Carlo and HPLC methods
Series Name/Journal:Acta Universitatis Agriculturae Sueciae
Year of publishing :2022
Number:2022:10
Number of Pages:64
Publisher:Swedish University of Agricultural Sciences
ISBN for printed version:978-91-7760-895-0
ISBN for electronic version:978-91-7760-896-7
ISSN:1652-6880
Language:English
Publication Type:Doctoral thesis
Article category:Other scientific
Version:Published version
Full Text Status:Public
Subjects:(A) Swedish standard research categories 2011 > 4 Agricultural Sciences > 401 Agricultural, Forestry and Fisheries > Agricultural Science
(A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Botany
Keywords:gliadin, glutenin, super-absorbents, LMW-GS, HMW-GS, protein modelling, peptides, folding, lanthionine, lysinoalanine, disulphide
URN:NBN:urn:nbn:se:slu:epsilon-p-115912
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-115912
ID Code:27010
Faculty:LTV - Fakulteten för landskapsarkitektur, trädgårds- och växtproduktionsvetenskap
Department:(LTJ, LTV) > Department of Plant Breeding (from 130101)
Deposited By: SLUpub Connector
Deposited On:11 Feb 2022 14:25
Metadata Last Modified:11 Feb 2022 14:31

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