Abstract The paper discusses the issues of rational use of secondary collagen-containing raw material in the food industry, namely cattle by-products. The technology of obtaining collagen hydrolysate from this type of raw material with the subsequent freeze-drying is proposed, which maximizes the level of preservation of native properties and the expands the scope of its application. The paper presents the stages of obtaining lyophilized collagen hydrolysate by biomodification of frozen cattle lips and ears. The preparation of lyophilized collagen hydrolysate was carried out as follows: the lips and ears were preliminary washed in running tap water for 20 minutes in order to remove mucus and impurities, muscle and adipose tissue was also removed; after draining (15-20 minutes), the raw material was ground on a top with a grid diameter of 2-3 mm. At the next stage, the crushed lips and ears were treated with a solution of Protepsin enzyme preparation in the ratio of the raw material to solution 1:2 and kept for 0.5-1.5 hours at a concentration of the enzyme preparation of 0.06% by weight of the raw material, while stirring periodically (at 17-22 °C). The filtrate from the product was separated on a sieve. Processed as described above, the raw material was subjected to freeze-drying. Evaluation of the temperature and duration of freeze-drying of collagen hydrolysate was carried out at a drying layer thickness of 5.0 mm and different drying temperatures: 20 °C, 30 °C, 40 °C, and 50 °C.

Abstract Protepsin belongs to the class of acid proteinases, containing carboxyl groups in the active center. The preparation cleaves peptide bonds formed by aromatic amino acids (tyrosine, phenylalanine), and does not hydrolize esters and amides. Along with the proteolytic complex, Protepsin contains collagenase, lipase, and other digestive enzymes. The preparation is obtained according to the original technology through maceration of animal endocrine raw materials, followed by purification, concentration, isolation and freeze dehydration of the enzyme complex. The results of the laboratory studies of the proteolytic activity of enzyme preparations show that Protepsin, the preparation of animal origin with a proteolytic activity of 100 units/g, has the greatest collagenase activity in the biomodification of native collagen-containing raw materials.

Abstract The paper deals with the possibility of processing category 2 animal byproducts with a ferment preparation. We chose collagen-rich cattle lips and ears as the category 2 byproducts for our study. The selected samples were processed in the following sequence: fixation, rinsing with running water, densifying the samples, slicing into sections, dying sections, and enclosing the sections under cover glass. The pathohistomorphologic changes found in the control samples significantly differ both before the processing and after the use of the ferment preparation Protepsin, which caused destructive metabolic and hydrolytic processes in the dense connective tissue of the ear and lip framework and led to softening of the muscle parenchyma of the organs.