The results shown in Figure 2 show that the viscosity value [η] for collagen released during hydrolysis was 60 min and was 15.15, and its viscosity was high. The viscosity value [η] for collagen isolated during the 80 minute hydrolysis time was 12.35 and was found to have the optimal viscosity for producing composite biomaterials. The viscosity [η] for the collagen samples isolated within 90 and 120 minutes of hydrolysis time was 11.42 and 11.02, respectively (2.7 MPa low) causing difficulties such as low.
According to the scientific literature, the inherent viscosity of collagen with a natural three-helix structure should be at least 11 [16. P. 69]. As a result of the research, all collagen samples can be considered as evidence that the values of intrinsic viscosity [η] of dilute solutions of 6% acetic acid are in the range of 11.02-15.15, while maintaining the natural structure. In turn, the obtained data on the duration of the second hydrolysis process showed that it is possible to extract collagen from the raw material of the skin, retaining its natural structure.
During the study, at the time of the second hydrolysis of 60, 80, 90 and 120 minutes, an aqueous mass was obtained containing 5.5-6.2, 4.8-5.5, 4.2-4.6 and 3.8-4 .1% collagen, respectively. A decrease in the amount of collagen in raw materials with an increase in hydrolysis time was established. This is explained not only by the rupture of the non-helical part of collagen, but also by the violation of the three-helix structure with an increase in the hydrolysis time. Therefore, at a second hydrolysis time of 80 minutes, an aqueous mass containing 4.8-5.5% collagen was obtained, and this hydrolysis time was chosen for obtaining biomaterials because of its flexibility and ease of molding. As a result of the research, it was found that the values of the intrinsic viscosity of solutions [η] range from 11.02 to 15.15 while three helical structures are preserved.
Collagen is a protein substance of natural nature and consists of a set of amino acids linked by peptide bonds. The structure and function of collagen depend on the specific amount of amino acids it contains. In our study, the qualitative and quantitative analysis of amino acids derived from collagen isolated from bovine skin was studied in the scientific literature by comparative comparison with the amino acids of collagen isolated from bovine skin. To do this, after acid hydrolysis of the amino acid composition of collagen by the Cohen method, PTC-derivatives of amino acids were synthesized and a qualitative and quantitative analysis was carried out using high-performance liquid chromatography (HPLC). The results are presented in table 4.
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