Purification and identification of dipeptidyl peptidase IV and angiotensin-converting enzyme inhibitory peptides from silver carp (Hypophthalmichthys molitrix) muscle hydrolysate
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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.
KeywordsSliver carp Dipeptidyl peptidase IV Angiotensin converting enzyme Dual inhibition
This study was supported by the National Science and Technology Ministry of China (Award number 2017YFD0400200) and the China Agriculture Research System (CARS-45).
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Conflict of interest
All author declares that they have no conflict of interest.
Compliance with ethics requirements
This article does not contain any studies with human or animal subjects.
- 6.Gillespie CD, Hurvitz KA (2013) Prevalence of hypertension and controlled hypertension—United States, 2007–2010. MMWR Surveill Summ 62 Suppl 3(3):144–148Google Scholar
- 7.World Health Organization (2013) A global brief on hypertension: silent killer, global public health crisis: world health day 2013. World Health Organization, GenevaGoogle Scholar
- 13.Lee SY, Sun JH (2017) Angiotensin converting enzyme inhibitory and antioxidant activities of enzymatic hydrolysates of korean native cattle (Hanwoo) myofibrillar protein. Biomed Res Int 2017(5):1–9Google Scholar
- 17.Zhang C, Zhang Y, Wang ZY, Chen SW, Luo YK (2017) Production and identification of antioxidant and angiotensin-converting enzyme inhibition and dipeptidyl peptidase IV inhibitory peptides from bighead carp (Hypophthalmichthys nobilis) muscle hydrolysate. J Funct Foods 35:224–235CrossRefGoogle Scholar
- 28.Zhang Y, Chen R, Ma H, Chen S (2015) Isolation and identification of dipeptidyl peptidase IV-inhibitory peptides from trypsin/chymotrypsin-treated goat milk casein hydrolysates by 2D-TLC and LC–MS/MS. J Agric Food Chem 63(40):9543–9549Google Scholar
- 31.Dai-Hung N, Bomi R, Se-Kwon K (2014) Active peptides from skate (Okamejei kenojei) skin gelatin diminish angiotensin-I converting enzyme activity and intracellular free radical-mediated oxidation. Food Chem 143(1):246–255Google Scholar
- 32.Bao C, Chen H, Cao L, Meng J, Jiangpeng (2016) Comparison of ACE inhibitory activity in skimmed goat and cow milk hydrolyzed by alcalase, flavourzyme, neutral protease and proteinase K. Acta Univ Cibiniensis 20(1):77–84Google Scholar
- 41.Martin RA, Cleary DL, Guido DM, Zurcher-Neely HA, Kubiak TM (1993) Dipeptidyl peptidase IV (DPP-IV) from pig kidney cleaves analogs of bovine growth hormone-releasing factor (bGRF) modified at position 2 with Ser, Thr or Val. Extended DPP-IV substrate specificity? BBA Protein Struct M 1164(3):252–260CrossRefGoogle Scholar
- 42.Wang TY, Hsieh CH, Hung CC, Jao CL, Chen MC, Hsu KC (2015) Fish skin gelatin hydrolysates as dipeptidyl peptidase IV inhibitors and glucagon-like peptide-1 stimulators improve glycaemic control in diabetic rats: a comparison between warm- and cold-water fish. J Funct Foods 19:330–340CrossRefGoogle Scholar
- 43.Liao P, Lan X, Liao D, Sun L, Zhou L, Sun J, Tong Z (2018) Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from the enzymatic hydrolysate of Carapax trionycis (the shell of the turtle Pelodiscus sinensis). J Agric Food Chem 66:7015–7022CrossRefGoogle Scholar
- 47.Fitzgerald RJ, Meisel H (2000) Milk protein-derived peptide inhibitors of angiotensin-I-converting enzyme. Br J Nutr 84(1):33–37Google Scholar