Angiotensin I-converting enzyme inhibitory activity of enzymatic hydrolysates of goat milk protein fractions

作者：Javier Espejo Carpio F; De Gobba Cristian; Guadix Antonio; Guadix Emilia M; Otte Jeanette^*

来源：International Dairy Journal, 2013, 32(2): 175-183.

DOI：10.1016/j.idairyj.2013.04.002

Casein and whey protein fractions from goat milk were hydrolysed by subtilisin and trypsin, individually and in combination, to release angiotensin converting enzyme (ACE)-inhibitory peptides. Selected hydrolysates were fractionated by size exclusion chromatography (SEC) and further characterised. The highest ACE-inhibitory activity was obtained from the casein fraction hydrolysed by the combination of enzymes. SEC presented 4 fractions with fraction F2 (%26lt;2.3 kDa) containing the highest concentration of peptides and the highest activity. F2 contained a number of peptides not previously identified from caprine caseins but with structural similarity to other ACE-inhibitory peptides. The most active fraction in relation to protein content was F4 with IC50 between 9.3 and 5.1 mu g mL(-1). This fraction contained a compound tentatively identified as WY, an active dipeptide not previously reported from caseins. The high inhibitory capacity of these fractions points towards the advantage of implementing a membrane process to concentrate the most active peptides.

• 出版日期2013-10