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Wheat flour proteins: isolation and functionality of gliadin and HMW‐glutenin enriched fractions
Author(s) -
Mimouni Brahim,
Robin Jean Michel,
Azanza JeanLouis,
Raymond Jacques
Publication year - 1998
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/(sici)1097-0010(199811)78:3<423::aid-jsfa135>3.0.co;2-6
Subject(s) - glutenin , gliadin , chemistry , chromatography , gluten , solubility , food science , plant protein , ethanol precipitation , biochemistry , organic chemistry , protein subunit , extraction (chemistry) , gene
The amount of glutenin subunits of high molecular weight (HMW‐glutenins) appears to be closely related to breadmaking. The relationship of their specific 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 Na 2 SO 3 , the procedure uses solubilisation in hot aqueous ethanol with the subsequent specific precipitation of HMW‐glutenins 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 (purification factor ∽12), whereas the supernatant mainly contained gliadins and LMW‐glutenins. After addition of these fractions to meal the modifications of the rheological properties of the resulting dough were investigated. A model explaining the participation of the different fractions to the structure and the solubility of gluten is suggested. © 1998 Society of Chemical Industry.