Strategies for the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in an enzymatic hydrolyzate of α-lactalbumin. Issue 8 (13th July 2016)

• Record Type: Journal Article
• Authors: Nongonierma, Alice B.; Le Maux, Solène; Hamayon, Joël; FitzGerald, Richard J.
• Is Part Of: Food & function. Volume 7:Issue 8(2016)
• Page Start: 3437
• Page End: 3443
• Publication Date: 2016-07-13
• Subjects: Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; Nutrition -- Periodicals; 664.07
• DOI: 10.1039/c6fo00239k
• Languages: English
• ISSNs: 2042-6496

Abstract

Abstract : Targeted enzymatic digestion to release DPP-IV inhibitory peptides from α-lactalbumin. Abstract : Bovine α-lactalbumin (α-La) contains numerous dipeptidyl peptidase IV (DPP-IV) inhibitory peptide sequences within its primary structure. In silico analysis indicated that the targeted hydrolysis of α-La with elastase should release DPP-IV inhibitory peptides. 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 highest mean DPP-IV inhibition value at 3.1 mg mL −1 of 75.8 ± 3.7% and had a half maximal DPP-IV inhibitory concentration (IC50 ) value of 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 preliminary 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.