Preparation of Type II Collagen Short Peptides: Temperature Conditions of Cartilage Homogenization and Collagen Hydrolysis.

Physicochemical properties of hyaline cartilage homogenates were studied by the method of microcalorimetry. Collagen hydrolysates were obtained after homogenization of hyaline cartilages under high pressure conditions at the temperatures that denaturate collagen. Thermodynamic parameters of thermal transition of collagen in cartilage suspension were determined.

Collagen Peptides from Hyaline Cartilage for the Treatment and Prevention of Joint Diseases: Isolation and Characteristics.

We studied the effects of Chymopsin and Caripazim on the proteolysis of collagen proteins from cattle tracheal hyaline cartilage. Homogenization of the cartilage under conditions of high pressure and temperature facilitated subsequent enzymatic hydrolysis: the degree of hydrolysis increased upon elevation of pressure from 40 to 80 mPa and temperature from 60 to 70°C. Proteolysis with Chymopsin yielded collagen peptides with molecular weights from 900 to 7000 Da, while Caripazim processing yielded collagen peptides with lower molecular weights from 250 to 780 Da consisting of 2-8 amino acids, which could be easily absorbed and intensely incorporated in the formation of the joint tissue structures.

Development of Low-Molecular Weight Collagen Peptide Complex with Glycosaminoglycan Components.

Enzymatic hydrolysis of biopolymers of the cartilage tissue was studied for obtaining a complex of type II collagen peptides and glycosaminoglycan oligosaccharides. Hydrothermal hydrolysis in a high pressure homogenizer followed by enzymatic hydrolysis of the cartilage tissue biopolymers with proteolytic enzyme preparation Karipazim yielded a complex of collagen peptides and glycosaminoglycan oligosaccharides with molecular weights of 240-720 Da. Low molecular weight of the components increases their bioavailability.