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ACTUAL ASPECTS OF THE USE OF METALLOPROTEINAS IN THE MEAT INDUSTRY FOR EFFECTIVE RESOURCE CONSERVATION

Irina Artemeva

Abstract

Matrix metalloproteinases (MMP) belong to the family of zinc metalloprotenases, whose function is related to the metabolism of the extracellular matrix proteins. These enzymes play an important role in the development of physiological processes such as morphogenesis, resorption and tissue remodeling, migration, adhesion, cell differentiation and proliferation, as well as in pathological conditions (rheumatoid arthritis, glomerulonephritis, periodontitis, ulceration of the cornea, etc.). To the first, the most studied class are collages. Currently, four representatives of this family are known: interstitial collagenase, or type I collagenase (MMP-1), neutrophil collagenase (MMP-8), collagenase 3 (MMP-13), collagenase 4 (MMP-18). MMP-1 is the first tissue enzyme that hydrolyzes the spiral region of collagen. MMP-1 is synthesized by a number of cells: normal and transformed fibroblasts, chondrocytes, epithelial cells, macrophages. MMP-8 was discovered in neutrophils, for which it received the name of neutrophilic collagenase. MMP-3 is found in breast carcinoma cells, as well as in rodent bone tissue cells. Collagenase was named for its ability to hydrolyze native collagen in the helical region. All four MMPs hydrolyze interstitial collagens. One of the current trends in solving this problem is the involvement of non-traditional and secondary sources of the meat and dairy industries, enriched with youth protein "collagen", in the technological process. Fundamental studies of a number of scientists substantiated the similarity of the physiological effects of dietary fiber and collagen. However, the use of collagen containing raw materials in the meat industry remains very limited due to the low digestibility and digestibility of this protein. To eliminate this problem, new ways of its modification are being developed. According to literature data, untransformed connective tissue improves protein absorption. At the same time, the transformed collagen is a building material for tissue repair. The article presents new data on the biomodification of the food industry collagen by metalloproteinases.

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