Šiuolaikinių proteominių metodų taikymas pramoniniam glitimo išskyrimo procesui valdyti ; Modern proteomic methods for control of industrial wheat gluten extraction

Wheat is one of the three most important crops in the world due to its value as a major food source and its unique suitability for bread production. This is due to their protein properties. Wheat grain proteins are divided into albumins, globulins and reserve, called gluten proteins, which are made up of gliadins and glutenins. The aim of this project is to determine the protein composition in gluten samples and to evaluate the application of proteomic methods to control the industrial gluten release process. Various methodologies in the field of proteomics have been applied in the work, such as: reversed-phase high-performance liquid chromatography - mass spectrometry, spectrophotometry, capillary electrophoresis, as well as Dhaka, Diuma and modified Osborne method and moisture determination method. The Dhaka methodology has been found to be suitable for process control and protein separation in higher yields, in contrast to the Osborne methodology. Using capillary electrophoresis, it was found that both extraction solutions used dissolve dry gluten proteins equally. It has been found that measurements of ultraviolet light absorption at 280 nm do not allow the determination of the exact protein concentration. Comparing the results of protein analysis with “Synapt G2S” and “LTQ Orbitrap XL” mass spectrometers, it was found that both methods are suitable for general gluten protein analysis and control of gluten release process, only “Synapt G2S” mass spectrometer data are more accurate. From the nitrogen content in the flour sample, the protein concentration was determined by the Diuma method to be suitable for the determination of the protein content and also for the control of the process, as the results obtained are in line with the literature data.