Identification of dipeptidyl peptidase-IV inhibitory peptides from mare whey protein hydrolysates

• Published in: Journal of dairy science Vol. 100; no. 9; pp. 6885 - 6894
• Main Authors: Song, J.J., Wang, Q., Du, M., Ji, X.M., Mao, X.Y.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.09.2017
• Subjects: Amino Acid Sequence; Animals; bioactive peptide; Diabetes Mellitus, Type 2 - drug therapy; dipeptidyl peptidase IV; Dipeptidyl-Peptidase IV Inhibitors - isolation & purification; Female; Horses; Hydrolysis; mare milk; Peptides - isolation & purification; Protein Hydrolysates - chemistry; Whey - chemistry; whey protein; whey protein; dipeptidyl peptidase IV; bioactive peptide; mare milk
• ISSN: 0022-0302; 1525-3198
• DOI: 10.3168/jds.2016-11828

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 β-lactoglobulin 1 f(71–77) and β-lactoglobulin 1 f(143–155), demonstrated DPP-IV inhibitory activity with half-maximal inhibitory concentrations of 86.34 and 69.84 μM, 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.