Hence, some synthetic drugs use DPP-IV inhibitory activity for the treatment of diabetes type II, but with significant side effects such as hypoglycemia, weight gain, increased bowel movement frequency, diarrhea, nausea, and abdominal pain 6. 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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