![]() ![]() Some di/tri/tetrapeptides with a proline at their C-terminus can suppress the dipeptidyl peptidase IV (DPP-IV) enzyme, which participates in the incretin hormone processing 3 and can regulate diabetes mellitus type II 4, 5. Gelatin can be applied in food and pharmaceutical industries however, bioactive peptides derived from this glycine and proline-rich protein 1, 2 can be more advantageous. Gelatin is a hydrocolloid that can be produced by partial hydrolysis of collagen from different sources, including fish byproducts, which represents an economical or environmental advantage. ![]() Moreover, the binding energy was sufficient for all three peptides to inhibit both ACE and DPP-IV enzymes with excellent three-dimensional conformation (RMSD = 0.000) for all six docking mechanisms. The synthesized peptides demonstrated multifunctional properties, which were further confirmed by in silico protocols. The antibacterial activity against both gram-negative and -positive food-borne pathogens, including Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Klebsiella pneumoniae, as well as the inhibitory potential of angiotensin-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV), was accessed in vitro. Bioactive peptides were produced from mackerel byproducts via successive enzymatic hydrolysis reactions using subtilisin A and actinidin as microbial and herbal proteases. Here, the biological characterization of these peptides was performed to engineer multifunctional peptides. ![]() The multifunctional properties of fish gelatin hydrolysates have not been completely elucidated. ![]()
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