Activities and sequences of the angiotensin I‐converting enzyme (ACE) inhibitory peptides obtained from the digested lentil (Lens culinaris) globulins. (12th July 2013)

• Record Type: Journal Article
• Authors: Jakubczyk, Anna; Baraniak, Barbara
• Is Part Of: International journal of food science & technology. Volume 48:Number 11(2013:Nov.)
• Page Start: 2363
• Page End: 2369
• Publication Date: 2013-07-12
• Subjects: Food industry and trade -- Periodicals; 664
• DOI: 10.1111/ijfs.12226
• Languages: English
• ISSNs: 0950-5423

Abstract

<abstract abstract-type="main" id="ijfs12226-abs-0001"> <title>Summary</title> <p>The aim of this study was the identification of potentially bioaccessible ACE‐inhibitory peptides obtained by <italic>in vitro</italic> gastrointestinal digestion of lentil globulins. ACE‐inhibitory peptides were purified by ion exchange chromatography and gel filtration. After the first step of purification, three peptide fractions with potential antihypertensive properties were obtained and the highest inhibitory activity was determined for the fraction 5 (IC₅₀ = 0.02 mg mL⁻¹). This fraction was separated on Sephadex G10, and six peptide fractions were obtained. The peptides of fraction (5‐F) with the highest potential antihypertensive activity (IC₅₀ = 0.13 mg mL⁻¹) were identified using ESI‐MS/MS. The sequences of peptides were KLRT, TLHGMV and VNRLM. Based on Lineweaver–Burk plots for the fraction 5‐F, the kinetic parameters as <italic>K</italic>_m (1.24 m<sc>m</sc>), <italic>V</italic>_max (0.012 U min⁻¹), <italic>K</italic>_i (0.12 mg mL⁻¹) and mode of inhibition were determined.</p> </abstract>