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GrainGenes Reference Report: CCM-77-702

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Reference	CCM-77-702
Title	Contribution of hydrophobic soluble gluten proteins, fractionated by hydrophobic interaction chromatography in highly acetylated agarose, to dough rheological properties
Journal	Cereal Chemistry
Year	2000
Volume	77
Pages	702-707
Author	Torres PI Vazquez-Moreno L Ledesma-Osuna AI Medina-Rodriguez C
Abstract	Summary: Hydrophobic interaction chromatography with highly acetylated agarose in 1-mL columns was used to fractionate gliadins and acid-soluble glutenins. Proteins were eluted in two fractions, the first with acetate buffer (pH 3.6) containing 35% propanol, and the second with Tris buffer in 8M urea. The proportion of eluted protein in the second fraction was called the surface hydrophobicity index. The study included 20 wheat samples of different baking qualities. Multiple regression analysis using the general linear model combined with the stepwise technique was used to relate the surface hydrophobicity index of soluble gluten proteins to specific dough rheological characteristics. Surface hydrophobicity index of gliadins and acetic acid soluble glutenins explained part of the variability of swelling index, extensibility, and work of deformation (dough strength) measured with the alveograph, and part of the farinograph water absorption variability, but showed no relationship to dough mixing characteristics. Hydrophobic soluble gluten proteins fractionated by hydrophobic interaction chromatography (HIC) explained a part of the variability of dough rheological properties
Keyword	[ Hide all but 1 of 30 ] acetate alveograph baking baking quality chromatography dough extensibility flour fraction gliadin gluten gluten proteins glutenin hydrophobicity mixing model molecular-weight subunit ph purification quality quantitation regression regression analysis rheological properties salts surface urea variability water wheat gluten

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