Collagen Hydrolysed from Maral Raw Material: Production Technology and Biochemical Composition

Collagen has a complex beneficial effect on human health, which makes it a popular component in various therapeutic diets. Deer antlers are a promising source of collagen. It has been used in traditional Chinese medicine for more than 20 centuries as an additive that supports the musculoskeletal system. The article describes the effect of extraction technology on the amino acid and biochemical composition of collagen obtained from the Altai wapiti, or maral (Cervus Canadensis). The research featured hydrolysates obtained from ground skin and tendons of ten marals. The mass fraction of collagen was determined by the concentration of oxyproline. The yield of dry solids was calculated in line with State Standard GOST 316402012. The method of atomic adsorption spectroscopy made it possible to calculate the mass concentration of macro- and microelements. Amine nitrogen was detected by formol titration while the general amino acid composition was studied using the method of high-performance liquid chromatography. The list of amino acids included glycine (14.36 g/100g), proline (8.87 g/100g), and oxyproline (7.83 g/100 g). Their concentration depended on the production technology. The content of arginine and lysine increased 4–5 times during fermentation and 1.5–2.3 times during high-temperature extraction of oxyproline, glutamic acid, and threonine. A step-by-step hydrolysis protocol with fermentation and high-temperature extraction provided the maximal yield of dry solids and amino acids. In this study, the collagen hydrolyzed from maral skin and tendons was rich in glycine, proline, and oxyproline, which makes it a prospective additive to be used in products that lack these amino acids. The effect of hydrolyzed maral collagen on the human body needs further research