Journal
JOURNAL OF FUNCTIONAL FOODS
Volume 29, Issue -, Pages 77-83Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jff.2016.12.005
Keywords
Chicken breast; In vitro digestion; Bioactive peptide; Angiotensin converting enzyme
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Funding
- Royal Golden Jubilee Scholarship [PhD/0223/2552]
- Suranaree University of Technology (SUT)
- Office of the Higher Education Commission under NRU project of Thailand
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The release of encrypted angiotensin converting enzyme (ACE) inhibitory peptides upon simulated in vitro gastrointestinal (GI) digestion of Korat crossbred (KC) and commercial broiler (BR) breast meat varied with cooking methods. Digestas of KC breast meat heated at 70 degrees C for 0.5 h (H-0.5) showed the highest ACE inhibitory activity, while digestas of KC chicken heated at 121 degrees C for 1 h showed the lowest inhibitory activity. ACE inhibitory activity varied with the protein digestibility. After a series of chromatographic techniques, we identified KPLLCS, ELFTT, and KPLL, novel potent ACE inhibitor peptides whose sequences were homologous to that of myosin and whose IC50 values were 0.37, 6.35 and 11.98 pM, respectively. ELFTT and KPLL were resistant to plasmin hydrolysis for up to 60 min. Therefore, KC chicken meat heated at H-0.5 could serve as a source of ACE inhibitory peptides upon GI digestion. (C) 2016 Elsevier Ltd. All rights reserved.
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