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Fourier spectroscopy of sarcoplasmic, myofibrillar, and connective tissue proteins of pork muscle tissue

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The study of sarcoplasmic proteins, actomyosin complex, and stroma of pork muscle tissue isolated by sequential water, salt (Weber's solution), and alkaline (0.6 M NaOH) extraction was performed using IR spectroscopy of disturbed total internal reflection. Sarcoplasmic and myofibrillar proteins were precipitated from the extracts with a three-fold excess of 96% ethanol or 5% trichloroacetic acid solution. Connective tissue proteins were obtained by removing the mucopolysaccharide complex from the stroma by alkaline treatment. The spectral difference between globular and myofibrillar proteins due to the nature of precipitating reagents which allow differentiating the absorption bands of sarcoplasmic globular proteins – albumins (1620 cm-1), globulins (1652 cm-1), and actomyosin complex proteins – actin andmyosin (1623 and 1660 cm-1. respectively) – is shown. Peptides isolated from supernatants with ethanol after separation by centrifugation of proteins precipitated with trichloroacetic acid always appeared in the region of 1590 cm-1. Vibrational spectra of dry protein samples were obtained using Tenzor-37 spectrometer in the wave number range of 4000–600 cm-1. Comparative use of different drying methods (air, microwave, and freeze-drying) demonstrated the need to take into account component composition of the source material and the compatibility of the nature of the precipitator and the drying method in the production of target products for a specific sphere of consumption.

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