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Purification and identification of dipeptidyl peptidase IV and angiotensin-converting enzyme inhibitory peptides from silver carp (Hypophthalmichthys molitrix) muscle hydrolysate
- Zhang, Yuqi, Liu, Huaigao, Hong, Hui, Luo, Yongkang
- European food research & technology 2019 v.245 no.1 pp. 243-255
- Hypophthalmichthys molitrix, diabetes, dipeptidyl-peptidase IV, food research, human health, hydrolysates, hypertension, inhibitory concentration 50, liquid chromatography, muscle protein, muscles, peptides, peptidyl-dipeptidase A, tandem mass spectrometry
- Diabetes and hypertension are increasing threats to human health, which could be improved by inhibiting dipeptidyl peptidase IV (DPP-IV) and angiotensin-converting enzyme (ACE), respectively. Herein, we used five different enzymes to hydrolyze silver carp (Hypophthalmichthys molitrix) muscle protein. Among all treatments, the Neutrase-generated hydrolysate that was purified by a three-step isolation and then was identified using liquid chromatography–tandem mass spectrometry resulted in the most potent DPP-IV inhibitory activity and relatively high ACE inhibitory activity. The identified peptide Ala-Ala-Leu-Glu-Gln-Thr-Glu-Arg was the most effective at inhibiting DPP-IV with a half-maximal inhibitory concentration (IC₅₀) value of 647.02 ± 4.30 µM. Leu-Leu-Asp-Leu-Gly-Val-Pro showed the highest ACE inhibitory activity with an IC₅₀ value of 329.33 ± 15.53 µM. Lys-Ala-Val-Gly-Glu-Pro-Pro-Leu-Phe exhibited the dual inhibition against both DPP-IV and ACE with IC₅₀ values of 1,317.39 ± 20.93 µM and 726.01 ± 8.69 µM, respectively. Interestingly, it seemed that the majority of peptides which were responsible for inhibiting DPP-IV were different from the ones which caused the inhibition of ACE.