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Abstract:
The interactions occurring in the protein complex of wheat dough have been characterized by the extraction and molecular sieving techniques supported with optical methods as well as with some rheological examinations. The effects of wheat albumin, soya globulin and beta-lactoglobulin preparations have been determined. The interactions of dough protein complex with soluble pentosans isolated from rye flour and with lipid fractions of wheat embryo were analysed as well. In most cases the advanced aggregation, leading to formation of high molecular weight product similar to glutenin fraction and the increase of insoluble protein fraction were observed. The albumin, globulin and gluten type proteins participated in the interactions. The beta-lactoglobulin generally caused an intense disaggregation of the dough protein complex. The increase of low molecular weight fraction contents was, however, accompanied with formation of some quantities of the high molecular weight complex.