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Production of novel ACE inhibitory peptides from beta-lactoglobulin using Protease N Amano

Ortiz-Chao, P., Gomez-Ruiz, J.A., Rastall, R.A., Mills, D., Cramer, R., Pihlanto, A., Korhonen, H. and Jauregi, P. (2009) Production of novel ACE inhibitory peptides from beta-lactoglobulin using Protease N Amano. International Dairy Journal, 19 (2). pp. 69-76. ISSN 0958-6946

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To link to this article DOI: 10.1016/j.idairyj.2008.07.011

Abstract/Summary

Potent angiotensin l-converting enzyme (ACE) inhibitory peptide mixtures were obtained from the hydrolysis of beta-lactoglobulin (beta Lg) using Protease N Amano, a food-grade commercial proteolytic preparation. Hydrolysis experiments were carried out for 8 h at two different temperatures and neutral pH. Based on their ACE inhibitory activity, samples of 6 h of digestion were chosen for further analysis. The temperature used for the hydrolysis had a marked influence on the type of peptides produced and their concentration in the hydrolysate. Protease N Amano was found to produce very complex peptide mixtures; however, the partially fractionated hydrolysates had already very potent ACE inhibitory activity. The novel heptapeptide SAPLRVY was isolated and characterised. It corresponded to beta Lg f(36-42) and had an IC50 value of 8 mu m, which is considerably lower than the most potent ACE inhibitory peptides derived from bovine beta Lg reported so far. (C) 2008 Elsevier Ltd. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences
Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences
ID Code:13109
Uncontrolled Keywords:ANGIOTENSIN-CONVERTING ENZYME, BIOACTIVE PEPTIDES, IDENTIFICATION, SEQUENCES, PROTEINS, FRAGMENT

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