Journal
JOURNAL OF DAIRY SCIENCE
Volume 100, Issue 9, Pages 6885-6894Publisher
ELSEVIER SCIENCE INC
DOI: 10.3168/jds.2016-11828
Keywords
dipeptidyl peptidase IV; mare milk; whey protein; bioactive peptide
Funding
- Key Projects in the National Science & Technology Pillar Program during the Twelfth Five-year Plan Period (China) [2013BAD18B12-05]
- National Natural Science Foundation of China [31371753]
- National Dairy Industry Technology System-Beijing Innovation Team (NDITS-BIT
- China)
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Inhibition of dipeptidyl peptidase-IV (DPP-IV) activity is a promising strategy for treatment of type 2 diabetes. In the current study, DPP-IV inhibitory peptides were identified from mare whey protein hydrolysates obtained by papain. The results showed that all the mare whey protein hydrolysates obtained at various hydrolysis durations possessed more potent DPP-IV inhibitory activity compared with intact whey protein. The 4-h hydrolysates showed the greatest DPP-IV inhibitory activity with half-maximal inhibitory concentration of 0.18 mg/mL. The 2 novel peptides from 4-h hydrolysate fractions separated by successive chromatographic steps were characterized by liquid chromatography electrospray ionization tandem mass spectrometry. The novel peptides Asn-Leu-Glu-Ile-Ile-Leu-Arg and Thr-Gln-Met-Val-Asp-Glu- Glu-Ile-Met-Glu-Lys-Phe-Arg, which corresponded to beta-lactoglobulin 1 f(71-77) and 13-lactoglobulin 1 f(143-155), demonstrated DPP-IV inhibitory activity with half-maximal inhibitory concentrations of 86.34 and 69.84,mu M, respectively. The DPP-IV inhibitory activity of the 2 peptides was retained or even improved after simulated gastrointestinal digestion in vitro. Our findings indicate that mare whey protein-derived peptides may possess potential as functional food ingredients in the management of type 2 diabetes.
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