Wheat flour proteins: isolation and functionality of gliadin and HMW-glutenin enriched fractions

✍ Scribed by Mimouni, Brahim; Robin, Jean Michel; Azanza, Jean-Louis; Raymond, Jacques

• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 279 KB
• Volume: 78
• Category: Article
• ISSN: 0022-5142
• DOI: 10.1002/(sici)1097-0010(199811)78:3<423::aid-jsfa135>3.0.co;2-6

✦ Synopsis

The amount of glutenin subunits of high molecular weight (HMWglutenins) appears to be closely related to breadmaking. The relationship of their speciÐc functional properties and gluten quality has not been demonstrated. The difficulty in isolating non-denatured HMW-glutenins explains largely the lack of information. Investigations have been conducted to isolate HMW-glutenins without using denaturing agents such as SDS or urea. Using wholemeal treated in mild reducing conditions with the procedure uses solubilisation in Na 2 SO 3 , hot aqueous ethanol with the subsequent speciÐc precipitation of HMWglutenins at low temperature. Proteins present in the various extracts were anlaysed by SDS-PAGE and reverse-phase HPLC. The HMW-glutenins were obtained by precipitation at low temperature from ethanol extract (puriÐcation factor D12), whereas the supernatant mainly contained gliadins and LMWglutenins. After addition of these fractions to meal the modiÐcations of the rheological properties of the resulting dough were investigated. A model explaining the participation of the di †erent fractions to the structure and the solubility of gluten is suggested.

Society of Chemical Industry.