Bioactive peptides from goat colostrum: isolation, identification and in-silico characterization.

The objectives of the study are to identify bioactive peptides from goat colostrum and use in-silico analysis to describe their physicochemical properties. Total protein fractions in colostrum (1–3 days), transitional (4–20 days), and mature (after 25 days) goat milk samples were quantified in the biochemical studies. Colostrum (27.26 mg/ml), transitional (12.01 mg/ml), and mature (6.56 mg/ml) protein concentrations were measured. In comparison to the transitional and mature stages of goat milk, the results showed that protein fractions in the colostrum stage have the highest protein concentration. The fat, protein, lactose, total solids, and immunoglobulin percentages in goat colostrum are also high. In 2D electrophoresis, a total of 81 protein spots were observed between 6 and 72 kDa marker regions. Out of these 81 protein spots, about nine prominent quantitative protein spots numbered 12, 23, 25, 30, 34, 60, 75, 77 and 79 were analyzed through MALDI-TOF/MS and they were identified as K casein, Alpha Lactalbumin, Ferritin, Calmodulin dependent protein kinase, Prolactin, Lactoferrin, Lactoperoxidase, Lysozyme and Alpha-S2-casein proteins respectively. The molecular weights of K casein, Lactoferrin, Lactoperoxidase, and Alpha-S2-casein proteins were determined using in silico physicochemical characterisation to be 69564.89 kDa, 21455.34 kDa, 80365.85 kDa, and 26388.09 kDa, respectively. These proteins contain a higher concentration of alpha helices, extended strands, beta twists, and random coils, according to their secondary structure. The findings of this study will aid future research into the isolation of bioactive peptides and their biological roles. [ABSTRACT FROM AUTHOR]