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. ORCID: https://orcid.org/0000-0002-8037-2511, 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 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
URI	https://reading-clone.eprints-hosting.org/id/eprint/13109
Item Type	Article
Refereed	Yes
Divisions	Life Sciences Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences
Uncontrolled Keywords	ANGIOTENSIN-CONVERTING ENZYME, BIOACTIVE PEPTIDES, IDENTIFICATION, SEQUENCES, PROTEINS, FRAGMENT
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