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Mashkin M.N. Interaction of processing reagents of preparatory operations of tannery production with collagen: study of structure and age-related features of collagen structure. Journal of Clothing Science. 2024; 9(3). Available at: https://kostumologiya.ru/PDF/02TLKL324.pdf (in Russian).

Interaction of processing reagents of preparatory operations of tannery production with collagen: study of structure and age-related features of collagen structure

Mashkin Mikhail Nikolaevich
Moscow Aviation Institute (National Research University), Moscow, Russia
E-mail: mnmashkin@yandex.ru
ORCID: https://orcid.org/0000-0002-6734-4292
RSCI: https://elibrary.ru/author_profile.asp?id=112638

Abstract. The structure and age-related features of collagen structure during the interaction of processing reagents of the liming operation of the preparatory process dressing of leather with collagen of cattle Achilles tendon samples were studied by the method of nuclear magnetic resonance on hydrogen atoms. To determine the anisotropic motion of collagen polymer chains taking into account both age-related features and treatment during the liming process, a study was conducted of the mobility of collagen functional groups in samples treated with ash solutions for different orientations with angles of 0°, 54° 44′ and 90°, between the direction of the external magnetic field and the direction of collagen fibers. To study the dynamics of the composition of various collagen forms during aging, the difference spectrum of nuclear magnetic resonance on hydrogen atoms was determined as the difference between the spectral function of nuclear magnetic resonance on hydrogen atoms of absorption of samples of one of the age periods and the spectral function of nuclear magnetic resonance of absorption of the base sample. The conducted study by the method of nuclear magnetic resonance of the collagen structure during the interaction of samples of the Achilles tendon of cattle with reagents of processing solutions of the liming operation of the preparatory process of leather dressing allows us to draw the following conclusions: age-related changes in the interval from 0,7 to 8 years do not have a significant effect on the collagen structure of the bovine Achilles tendon; the use of the difference spectrum of nuclear magnetic resonance on hydrogen atoms allows us to obtain a quantitative assessment of collagen III in samples of the Achilles tendon of cattle.

Keywords: collagen; bovine achilles tendon; dermis; liming; nuclear magnetic resonance; collagen polypeptide chain; broad-band spectrum; polymer chain motion

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