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- W3083146307 endingPage "100748" @default.
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- W3083146307 abstract "Dipeptidyl peptidase IV (DPP-IV) has an important role in blood glucose metabolism. Silver carp swim bladder protein was hydrolyzed using papain, bromelain, Alcalase 2.4 L, Neutrase, and Flavourzyme. The swim bladder hydrolysate obtained using 5 h hydrolysis of Neutrase showed the highest DPP-IV inhibition (81 ± 2%) at 5 mg/mL. This hydrolysate was purified sequentially using ultrafiltration, gel filtration chromatography, and RP-HPLC. Peptide sequences from the RP-HPLC fractions were identified using liquid chromatography tandem mass spectrometry. The most potent DPP-IV inhibitory peptide WGDEHIPGSPYH (IC50: 0.35 ± 0.01 mM) showed an uncompetitive inhibition mode. Docking analysis showed that the binding site of WGDEHIPGSPYH was located inside the cavity of the DPP-IV monomer, which was close to the catalytic site. WGDEHIPGSPYH and its hydrolysate IPGSPY were transported intact across a Caco-2 cell monolayer. These two peptides were tested for their effects on Caco-2 and INS-1 cells and both showed good inhibition for soluble DPP-IV and promoted insulin secretion." @default.
- W3083146307 created "2020-09-11" @default.
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- W3083146307 date "2020-12-01" @default.
- W3083146307 modified "2023-09-30" @default.
- W3083146307 title "Identification and characterization of DPP-IV inhibitory peptides from silver carp swim bladder hydrolysates" @default.
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- W3083146307 doi "https://doi.org/10.1016/j.fbio.2020.100748" @default.
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