Novel Umami Peptide IPIPATKT with Dual Dipeptidyl Peptidase-IV and Angiotensin I-Converting Enzyme Inhibitory Activities.

A novel umami peptide, IPIPATKT, showed excellent dual dipeptidyl peptidase-IV (DPP-IV) and angiotensin I-converting enzyme (ACE) inhibitory activities, the IC values were 64 and 265 μM, respectively. Molecular docking displayed that IPIPATKT was docked into the S1 and S2 pockets of ACE, and it was close to the active site pocket of DPP-IV. The insulin-resistant-HepG2 (IR-HepG2) cell model and human umbilical vein endothelial cell (HUVEC) model showed that the peptide significantly increased the content of glucose, the activities of hexokinase, pyruvate kinase, and the concentration of nitric oxide ( < 0.

Isolation, characterization and molecular docking of novel umami and umami-enhancing peptides from Ruditapes philippinarum.

To understand the taste of the Ruditapes philippinarum, 14 novel umami peptides were isolated and identified by gel chromatography, HPLC and UPLC-ESI-QTOF-MS/MS. Separations were combined with sensory evaluations and electronic tongue determinations. The peptide sequences were GRVSNCAA, SEEK, KEMQKN, KSAEN, QIEELEGK, TDVEQEGD, HNESQN, RGEPNND, TGDPEK, KGGGGP, TYLPVH, PAATIPE, GPAGPAGPR and AGAGPTP.