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

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Markgren, JoelSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för växtförädling,Department of Plant Breeding (author)

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

BookEnglish2022

Publisher, publication year, extent ...

2022
Swedish University of Agricultural Sciences,2024

Numbers

LIBRIS-ID:oai:slubar.slu.se:115912
ISBN:9789177608950
ISBN:9789177608967
https://res.slu.se/id/publ/115912URI

Supplementary language notes

Language:English
Summary in:English

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SwePubSwePub

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Subject category:vet swepub-contenttype
Subject category:dok swepub-publicationtype

Series

Acta Universitatis Agriculturae Sueciae,1652-6880

Notes

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.

Subject headings and genre

LANTBRUKSVETENSKAPER Lantbruksvetenskap, skogsbruk och fiske Jordbruksvetenskap hsv//swe
AGRICULTURAL SCIENCES Agriculture, Forestry and Fisheries Agricultural Science hsv//eng
NATURVETENSKAP Biologi Botanik hsv//swe
NATURAL SCIENCES Biological Sciences Botany hsv//eng

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Sveriges lantbruksuniversitetInstitutionen för växtförädling (creator_code:org_t)
Sveriges lantbruksuniversitet

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AGRICULTURAL SCIENCES: AGRICULTURAL SCI ...; and Agriculture Fore ...; and Agricultural Sci ...

NATURAL SCIENCES: NATURAL SCIENCES; and Biological Scien ...; and Botany

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By the university: Swedish University of Agricultural Sciences

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