[Physicochemical properties of proteins from wheat grown under high-contrast climatic conditions].

Studies using electrophoresis, gel chromatography, viscometry, and calorimetry revealed an interrelation of several physicochemical properties of proteins of soft wheat grown under conditions of cool and wet weather with rheological characteristics of gluten and dough and bread quality. The ratio of gliadin and albumin-globulin polypeptides in flour with short-tearing gluten was much lower compared to that in flour with normal gluten. Proteins from flour with short-tearing gluten, including the water-soluble and salt-soluble fraction, had a loose spatial structure. Gluten fractions of this gluten (gliadin and glutenin) were characterized by a more compact and elongated structure compared to normal gluten. As distinct from normal gluten, the conformation of protein particles in short-tearing gluten depended little on hydrophobic interactions. The results suggest that the main components of grain determine the rheological properties of short-tearing gluten.

[Physicochemical properties and specific structural features of protein-lipid composites of increased nutritive value]. / Fiziko-khimicheskie svoistva i strukturnye osobennosti belkovo-lipidnykh kompozitov povyshennoi pishchevoi tsennosti.

Fractional and component compositions of protein-lipid composites with increased nutritive value (compared to the protein preparations from which they were produced) were studied based on solubility and electrophoretic behavior. Differences in the fractional compositions of proteins and the amounts of hydrogen, ionic, and hydrophobic bonds were found. It was demonstrated that the water-, salt-, and alkali-soluble fractions of proteins changed during the manufacturing of the composites with soybean and wheat bran flour; the water- and alkali-soluble fractions, with protein concentrate from bran. Heterogeneity of the compositions and specific conformational features of composite proteins resulting from disulfide bonds were found. It was demonstrated that, during the manufacturing of composites, proteins of soybean flour aggregated (with the involvement of disulfide bonds), whereas protein products from wheat bran disaggregated. Breaks of interchain (wheat) or intrachain (concentrate) disulphide bonds accompanied the disaggregation. Overall the properties and specific structural features of the protein-lipid composites studied depended on the nature of the protein (soybean or wheat), type of initial preparations (flour or concentrate), and method of their production (emulsifying or drying).

[Physico-chemical and structural changes gliadin and glutenin components of different qualities of gluten]. / Fiziko-khimicheskie i strukturnye razlichiia gliadinovykh i gliuteninovykh komponentov kleikoviny raznogo kachestva

By gel-chromatography on Sephadex and electrophoresis in polyacrylamide gel the structure and composition of gliadin and glutenin compounds of gluten from the strong and weak varieties of Saratovskaya 29 and Akmolinskaya 1 wheats were investigated. It was shown that similar protein fractions of strong and week gluten differed in the content of certain amino acids, number of disulphide bonds, electrophoretic mobility, ratio of components made of one and several polypeptide chains, molecular weight of individual components and subunits, and the content of high molecular weight proteins.