Production of novel ACE inhibitory peptides from β-lactoglobulin using Protease N AmanoOrtiz-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 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1016/j.idairyj.2008.07.011 Abstract/SummaryPotent 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.
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