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Strategies for the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in an enzymatic hydrolyzate of alpha-lactalbumin

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posted on 2017-04-13, 14:45 authored by Alice B. Nongonierma, Solène Le Maux, Joël Hamayon, Richard J. Fitzgerald
Bovine α-lactalbumin (α-La) contains numerous dipeptidyl peptidase IV (DPP-IV) inhibitory peptides sequences within its primary structure. In silico analysis indicated that the targeted hydrolysis of α-La with elastase should release DPP-IV inhibitory peptide sequences. An α-La isolate was hydrolysed with elastase under different conditions using an experimental design approach incorporating 3 factors (temperature, pH and enzyme to substrate ratio (E:S) ratio) at 2 levels. The hydrolyzate generated at pH 8.5, 50C, E:S 2.0% (w/w) (H9) displayed the lowest half maximal DPP-IV inhibitory concentration (IC50 = 1.20 ± 0.12 mg mL-1). Five α-La-derived DPP-IV inhibitory peptides (GY, GL, GI, NY and WL) predicted to be released in silico were identified by liquid-chromatography tandem mass spectrometry (LC-MS/MS) within H9 and its simulated gastrointestinal digestion (SGID) sample. This proof of concept study demonstrated the benefit of using a targeted approach combined with an experimental design in the generation of dietary protein hydrolyzates with DPP-IV inhibitory properties.

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Publication

Food and Function;7, pp. 3437-3443

Publisher

Royal Society of Chemistry

Note

peer-reviewed

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EI

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Personal use of this material is permitted. Permission from Royal Society of Chemistry must be obtained for all other uses

Language

English

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