4.4 Article

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

Journal

INTERNATIONAL DAIRY JOURNAL
Volume 32, Issue 2, Pages 175-183

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.idairyj.2013.04.002

Keywords

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Funding

  1. Consejeria de Innovacion, Ciencia y Empresa of Junta de Andalucia [P07-TEP-02579]
  2. Danish Strategic Research Council through the NOVENIA project

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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 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. (C) 2013 Elsevier Ltd. All rights reserved.

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