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Umami‐ and kokumi‐taste‐active peptides in Maillard reaction products of enzymatic hydrolysate of bovine bone marrow extract (BBME) were purified and identified by ultrafiltration, gel filtration chromatography, reverse‐phase high‐performance liquid chromatography, liquid chromatography/quadrupole‐time of flight mass spectrometry (LC‐Q‐TOF‐MS/MS) and sensory evaluation. Eight umami and kokumi taste oligopeptides were found in the enzymatic hydrolysate of BBME. After Maillard reaction, the numbers of oligopeptides increased to twelve, such as Ala‐His, Ala‐Val‐His, Gly‐Pro, His‐Gly, Pro‐Ala‐His, Pro‐Val‐Asn‐His, Phe‐Glu‐Ala, Ala‐Ala‐Cys‐Arg, Leu‐Met, Leu‐Thr‐His, Pro‐Gly‐His, Ser‐Thr‐Gly‐Arg, which are linked to a variety of functional properties, such as ACE inhibitor, prolyl endopeptidase inhibitor and dipeptidyl peptidase IV inhibitor, etc. Eight peptides, including Cys‐Pro‐Arg, Ser‐Gly‐Val‐Glu, Pro‐Cys, Cys‐Glu, Cys‐Met‐Thr, Phe‐Glu‐Ala, Ala‐Gln and Leu‐Met, were synthesised and then subjected to sensory evaluation. The evaluation showed that among the eight peptides, Cys‐Pro‐Arg, Pro‐Cys and Leu‐Met led to the distinctly enhanced kokumi taste in blank beef soup. The influence of enzymatic hydrolysis and Maillard reaction to taste‐active components in bovine bone extract including amino acids, nucleotide and peptides. [ABSTRACT FROM AUTHOR]

Summary: Inhibition of dipeptidyl peptidase IV (DPP‐IV) was considered to be a crucial target for type 2 diabetes, and food‐derived peptides were superior source of DPP‐IV inhibitory peptides. The purpose of this investigation was to identify inhibitory peptides from salmon skin collagen using simulated digestion combined with Caco‐2 cell monolayer membrane model. The analysis in silico showed that TKLPAVF and YLNF were potential inhibitory peptides. Determination of the inhibition activity showed that the IC50 values of TKLPVAF and YLNF were 242.10 ± 3.40 and 146.90 ± 4.40 µm, respectively. Molecular docking results showed that seven hydrogen bonds were formed between YLNF and key residues of DPP‐IV. YLNF may be considered a novel DPP‐IV inhibitory peptide. In addition, YLNF could be transported by Caco‐2 cell monolayer membrane in intact, and the apparent permeability coefficient value was (3.54 ± 0.34) × 10‐6 cm s−1 at 5 mm. [ABSTRACT FROM AUTHOR]