Home
Resources
Publications
Susceptibility of Milk Protein-Derived Peptides to Dipeptidyl Peptidase IV (DPP-IV) Hydrolysis

Susceptibility of Milk Protein-Derived Peptides to Dipeptidyl Peptidase IV (DPP-IV) Hydrolysis

Alice B Nongonierma, Richard J FitzGerald

Food Chem. 2014 Feb 15;145:845-52.

PMID: 24128555

Abstract:

In silico digestion of milk protein-derived peptides with gastrointestinal enzyme activities was used to predict the release of peptides with a Pro residue at position 2 from the N terminus. These peptides are known to act as preferred dipeptidyl peptidase IV (DPP-IV) substrates. Five casein-derived synthetic peptides (Ile-Pro-Ile-Gln-Tyr, Leu-Pro-Leu-Pro-Leu, Tyr-Pro-Tyr-Tyr, Leu-Pro-Tyr-Pro-Tyr and Ile-Pro-Ile) and a casein (CasH), whey (WPH) and lactoferrin hydrolysate (LFH) generated with gastrointestinal enzymes were incubated with DPP-IV at 37 °C for 18 or 24h. Peptide breakdown was evident following incubation with DPP-IV. Different modes of DPP-IV inhibition were observed depending on the test compound. Ile-Pro-Ile-Gln-Tyr, Tyr-Pro-Tyr-Tyr and Leu-Pro-Tyr-Pro-Tyr were substrate-, Leu-Pro-Leu-Pro-Leu and CasH were prodrug- while WPH and LFH were true DPP-IV inhibitors. These results are relevant for the bioactivity and bioavailability of functional foods targeting DPP-IV inhibition with potential blood glucose regulatory properties in humans.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP90614485	Ile-Pro-Ile		90614-48-5	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: