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Titolo:
Studies on the distribution and binding of endogenous glutathione in wheatdough and gluten. II. Binding sites of endogenous glutathione in glutenins
Autore:
Huttner, S; Wieser, H;
Indirizzi:
Deutsch Forsch Anstalt Lebensmittelchem, D-85748 Garching, Germany DeutschForsch Anstalt Lebensmittelchem Garching Germany D-85748 Germany Kurt Hess Inst Mehl & Eiweissforsch, D-85748 Garching, Germany Kurt Hess Inst Mehl & Eiweissforsch Garching Germany D-85748 ng, Germany
Titolo Testata:
EUROPEAN FOOD RESEARCH AND TECHNOLOGY
fascicolo: 6, volume: 213, anno: 2001,
pagine: 460 - 464
SICI:
1438-2377(200111)213:6<460:SOTDAB>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
DISULFIDE BONDS; CYSTINE PEPTIDES; GLIADINS;
Keywords:
wheat; gluten; glutathione; glutenins; binding sites;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
9
Recensione:
Indirizzi per estratti:
Indirizzo: Wieser, H Deutsch Forsch Anstalt Lebensmittelchem, Lichtenbergstr 4, D-85748 Garching, Germany Deutsch Forsch Anstalt Lebensmittelchem Lichtenbergstr4 Garching Germany D-85748
Citazione:
S. Huttner e H. Wieser, "Studies on the distribution and binding of endogenous glutathione in wheatdough and gluten. II. Binding sites of endogenous glutathione in glutenins", EUR FOOD RE, 213(6), 2001, pp. 460-464

Abstract

For the identification of the binding sites of glutathione (GS) in glutenins, flour of the wheat cultivar "Canadian Western Red Spring" was mixed with water containing S-35-labelled reduced GS as a tracer. The resulting dough was washed in a Glutomatic, and, in order to remove gliadins, the gluten obtained was extracted with 70% aqueous ethanol adjusted to pH 5.5 with acetic acid. The residual proteins (glutenins) were hydrolyzed with thermolysin, and the hydrolysate was separated by gel permeation chromatography on Sephadex G25 and by several steps of reversed-phase HPLC on C-18 silica gel. The major radioactive disulphide peptides identified by scintillation analysis were collected and analysed for their amino acid sequences. Twenty-fivepeptides linked to GS could be assigned to known sequences of gluten proteins. Most peptides (16) were derived from low molecular weight (LMW) subunits of glutenin. Among these, 13 peptides contained the cysteine residue C-b*, which is present in the repetitive sequence region of LMW subunits and which has been postulated to form intermolecular disulphide bonds. This peptide type represented 45% of the total radioactivity of isolated peptides. Three further peptides from LMW subunits representing 46% of radioactivity included cysteine C-x, which has also been proposed to form intermolecular disulphide bonds. Four peptides with 3.2% of radioactivity could be assignedto high molecular weight subunits (cysteines C-b, C-d, C-e, C-y) and four peptides (3.0% of radioactivity) to glutenin-bound gamma -gliadins (C-b*, C-w, C-z). One peptide (3.3% of radioactivity) corresponded to cysteine C-c from gamma -gliadins or LMW subunits. Altogether the cysteine residues in glutenins. which are usually linked by intermolecular disulphide bonds, contributed up to 95% of total radioactivity. The results obtained are in accordance with the effect of reduced GS on the rheological properties of dough,namely the weakening of dough by depolymerization of glutenin polymers viaspecific cleavage of intermolecular disulphide bonds.

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Documento generato il 25/02/20 alle ore 08:08:03