[Physicochemical properties of proteins from wheat grown under high-contrast climatic conditions].
作者： V. V. Kolpakova , E. N. Molchanova , A. V. Vasil’ev , L. V. Chumikina
DOI: 10.1134/S0003683807030180
关键词:
摘要: Studies using electrophoresis, gel chromatography, viscometry, and calorimetry revealed an interrelation of several physicochemical properties proteins soft wheat grown under conditions cool wet weather with rheological characteristics gluten dough bread quality. The ratio gliadin albumin-globulin polypeptides in flour short-tearing was much lower compared to that normal gluten. Proteins from gluten, including the water-soluble salt-soluble fraction, had a loose spatial structure. Gluten fractions this (gliadin glutenin) were characterized by more compact elongated structure As distinct conformation protein particles depended little on hydrophobic interactions. results suggest main components grain determine
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