Direct evidence that the number and location of cysteine residues affect glutenin polymer structure

M. P. Lindsay, L. Tamás, R. Appels, J. H. Skerritt

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

In this study, the possible roles of three well-characterised model prolamins in the structure of the glutenin macropolymer were examined. Model prolamins were labelled with fluorescein isothiocyanate (FITC), and incorporated into the glutenin macropolymer of a base flour using a partial reduction-oxidation scheme. The effect of incorporation of the model prolamins on dough behavior was determined by assessing differences in polymer size distribution, mixing properties, and distribution of the model prolamins in a dough after incorporation. Using this approach, the prolamins capable of forming inter-chain disulphide bonds were shown to be incorporated into the glutenin macropolymer, while prolamins that were not capable of forming inter-chain disulphide bonds were retained as monomers. The distribution of fluorescently-labelled prolamins after their incorporation into the glutenin macropolymer of the dough was examined by confocal light scanning microscopy, in order to determine the possible roles of ω-gliadins and glutenin-like subunits with varied cysteine residue compositions in the structural organisation. The role of the model prolamins was a function of the disulphide-bonding capabilities of the polypeptides. Model ω-gliadins were retained as monomers and functioned as space fillers; model glutenin-like subunits containing a single cysteine residue incorporated into the glutenin macropolymer but functioned as chain terminators; and model glutenin-like subunits containing two cysteine residues incorporated into the glutenin macropolymer and acted as chain extenders.

Original languageEnglish
Pages (from-to)321-333
Number of pages13
JournalJournal of Cereal Science
Volume31
Issue number3
DOIs
Publication statusPublished - May 2000

Fingerprint

Prolamins
glutenins
prolamins
Cysteine
cysteine
polymers
Polymers
dough
Disulfides
Gliadin
gliadin
disulfide bonds
Monomers
attachment behavior
filling materials
glutenin
isothiocyanates
Flour
fluorescein
Fluorescein

Keywords

  • C-hordein
  • Confocal light microscopy
  • Gluten
  • Glutenin
  • Labelling

ASJC Scopus subject areas

  • Agronomy and Crop Science
  • Food Science

Cite this

Direct evidence that the number and location of cysteine residues affect glutenin polymer structure. / Lindsay, M. P.; Tamás, L.; Appels, R.; Skerritt, J. H.

In: Journal of Cereal Science, Vol. 31, No. 3, 05.2000, p. 321-333.

Research output: Contribution to journalArticle

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