Release and identification of angiotensin-converting enzyme-inhibitory peptides as influenced by ripening temperatures and probiotic adjuncts in Cheddar cheeses |
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Authors: | L Ong NP Shah |
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Affiliation: | aSchool of Molecular Sciences, Victoria University, Werribee Campus, P.O. Box 14428, Melbourne, Victoria 8001, Australia |
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Abstract: | The aim of the study was to examine the release of angiotensin-converting enzyme (ACE)-inhibitory peptides in Cheddar cheeses made with starter lactococci and Bifidobacterium longum 1941, B. animalis subsp. lactis LAFTI® B94, Lactobacillus casei 279, Lb. casei LAFTI® L26, Lb. acidophilus 4962 or Lb. acidophilusLAFTI® L10 during ripening at 4 and 8 °C for 24 weeks. ACE-inhibitory activity of the cheeses was maximum at 24 weeks. Cheeses made with the addition of Lb. casei 279, Lb. casei LAFTI® L26 or Lb. acidophilus LAFTI® L10 had significantly higher (P < 0.05) ACE-inhibitory activity than those without any probiotic adjunct after 24 weeks at 4 and 8 °C. The IC50 of cheeses ripened at 4 °C was not significantly different (P > 0.05) to that ripened at 8 °C. The lowest value of the IC50 (0.13 mg mL−1) and therefore the highest ACE-inhibitory activity corresponded to the cheese with the addition of Lb. acidophilus LAFTI® L10. Several ACE-inhibitory peptides were identified as κ-CN (f 96–102), αs1-CN (f 1–9), αs1-CN (f 1–7), αs1-CN (f 1–6), αs1-CN (f 24–32) and β-CN (f 193–209). Most of the ACE-inhibitory peptides accumulated at the early stage of ripening, and as proteolysis proceeded, some of the peptides were hydrolyzed into smaller peptides. |
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Keywords: | Angiotensin-converting enzyme Cheddar cheese Probiotic bacteria Proteolysis |
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