MODELING OF ANIMAL PROTEIN HYDROLYSIS BY ENDOPROTEASES IN SILICO

Recently, there has been an increased demand for functional foods that promote health. Meat offal can serve as promising raw material for such kind of foods, for example, pork stomachs, rich in bioavailable protein. The purpose of this study was to evaluate the potential biological activity of various protein isolates of animal origin. The object of the study was protein identified in the UniProt database as VIP_PIG (P01284) or glucagon-like protein. Computer modeling was used to analyze the probability of bioactive peptides after protein hydrolysis using proteinase K, thermolysin and pepsin (pH>2). It was found that these proteases demonstrated a high potential in splitting protein into fragments. Pepsin (pH>2) promoted the formation of more peptides in hydrolysate. The longest peptide «FTSDFSR» was found in samples affected with thermolysin, at the same time, this peptide has the highest molecular weight (859.3944 kDa). The VKKY peptide was recognized as the most common in samples with all three enzymes, and was the first by weight (537.3395) when affected with pepsin (pH > 2). Subsequently, 6 bioactive peptides with peptide ranker scores above 0.5 were synthesized. Further work of the study will be aimed at determining toxicity, allergenicity, as well as the presence of therapeutic effect in silico and in vivo.