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KMID : 1161420190220121294
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Journal of Medicinal Food
2019 Volume.22 No. 12 p.1294 ~ p.1300
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Identification of Angiotensin I-Converting Enzyme-Inhibitory and Anticoagulant Peptides from Enzymatic Hydrolysates of Chicken Combs and Wattles
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Bezerra Taliana Kenia Alencar
de Lacerda Jose Thalles Jocelino Gomes
Salu Bruno Ramos
Oliva Maria Luiza Vilela
Juliano Maria Aparecida
Pacheco Maria Teresa Bertoldo
Madruga Marta Suely
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Abstract
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Peptides from protein hydrolysate of a mixture of chicken combs and wattles (CCWs) were obtained through enzymatic hydrolysis, and their anticoagulant and inhibitory effects on angiotensin I-converting enzyme (ACE) were investigated. The protein hydrolysate exhibited anticoagulant capacity by the intrinsic pathway (activated partial thromboplastin time) and potent ACE-inhibitory activity. The peptides were sequenced by LC-MS to identify those with higher inhibitory potential. From the pool of sequenced peptides, the following three peptides were selected and synthesized based on their low molecular weight and the presence of amino acids with ACE-inhibitory potential at the C-terminus: peptide I (APGLPGPR), peptide II (Piro-GPPGPT), and peptide III (FPGPPGP). Peptide III (FPGPPGP) showed the highest ACE-inhibitory capacity among the peptides selected. In conclusion, a peptide (FPGPPGP) of unknown sequence was identified as having potent ACE-inhibitory capacity. This peptide originated from unconventional hydrolysates from poultry slaughter waste, including combs and wattles.
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KEYWORD
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bioactive assays, chicken collagen, enzymatic proteolysis, peptide sequences, peptide synthesis
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