FEATURES OF THE SECONDARY STRUCTURE OF BSA - CONTAINING PROTEIN COMPLEXES, ISOLATED FROM MILK OF HIGH TEMPERATURE PROCESSING

Present paper describes features of the component composition in the secondary structure of BSA–containing protein complexes isolated from ultra-pasteurized (UHT), sterilized (SHT) and powdered (DRY) milk. We have found β – sheets to present in all complexes investigated. However, the smallest number of such components have been revealed in samples derived from sterilized milk with less β – sheets in 1621–1626 cm –1  region. The composition study of the complexes originated from UHT milk has shown random coils to be the rarest in them. When considering the structure of the complexes isolated from powdered milk, the α – 3 10 – heliсes were more characteristic for such samples, then the α – helix. Moreover, during spray–drying, the number of random structures increase with a simultaneous decrease in the number of β – sheets, whereas in UHT – and SHT – processing the number of random structures is inversely proportional to the number of α – helices.