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

Ortiz-Chao, P., Gómez-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 β-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 I-converting enzyme (ACE) inhibitory peptide mixtures were obtained from the hydrolysis of β-lactoglobulin (βLg) 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 βLg f(36–42) and had an IC50 value of 8 μm, which is considerably lower than the most potent ACE inhibitory peptides derived from bovine βLg reported so far.