IR spectroscopy method in the study of irradiated pork muscle tissue and its components
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One of the modern methods that allows to increase the long-term storage of meat products in fresh form by several times is their treatment with ionizing radiation. The purpose of this work was to study by IR spectroscopy of the disturbed total internal reflection of the effect of fast electron irradiation in radurization modes (6.5–25.0 kGr) on the optical characteristics of protein components of crushed native pork muscle tissue and its main solid–phase components (muscle fiber, stroma, and stroma proteins) and contact treatment (10 minutes) with 40% ethanol in a whole lump form. During the irradiation period, the samples were subjected to sequential fractionation by extraction with water-salt and alkaline extractants, which is based on a hierarchical sequence in the solubility of globular, myofibrillar, and stroma proteins. The isolated solid-phase components of muscle tissue were freeze-dried at –30°C and studied by vibrational spectroscopy in the range of 4000-600 cm-1 on a Fourier spectrometer Tpsog-37. Studies have shown that the dependences of changes in the optical properties of protein components, which were controlled by the intensity, shape, and position of the Amide-I and Amide-II bands, were periodic in nature and depend not only on the amount of radiation dose absorbed by the muscle tissue, but also on which component of the fractionated component they are. It is noted that in the spectra of stroma proteins, for which the position of the bands at 1640 and 1563 cm-1 is typical, a band of polypeptides (1590 cm-1) appears after irradiation, indicating partial destruction of their fibrils. The same bands were observed in the spectra of muscle tissue and fiber treated with ethanol after irradiation with a dose of 12.5 kGr. Pretreatment of muscle tissue with ethanol in whole chunks leads to stabilization of protein structures.
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