@misc{10481/87376,
year = {2013},
month = {4},
url = {https://hdl.handle.net/10481/87376},
abstract = {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 (<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 μg 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.},
organization = {Consejería de Innovación, Ciencia y Empresa of Junta de Andalucía (P07-TEP-02579)},
organization = {Danish Strategic Research Council (NOVENIA project)},
keywords = {ACE inhibitory peptides},
keywords = {Goat milk},
keywords = {Hydrolysis},
title = {Angiotensin I-converting enzyme inhibitory activity of enzymatic hydrolysates of goat milk protein fractions},
doi = {10.1016/j.idairyj.2013.04.002},
author = {Espejo Carpio, Francisco Javier and De Gobba, Cristian and Guadix Escobar, Antonio María and Guadix Escobar, Emilia María and Otte, Jeanette},
}