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Purification and Characterization of a Novel Angiotensin I-Converting Enzyme Inhibitory Peptide Derived from an Enzymatic Hydrolysate of Duck Skin Byproducts

2012; American Chemical Society; Volume: 60; Issue: 40 Linguagem: Inglês

10.1021/jf3023172

1520-5118

Seung‐Jae Lee, Yon-Suk Kim, Seong-Eun Kim, Eun‐Kyung Kim, Jin-Woo Hwang, Tae-Kyu Park, Bo Kyung Kim, Sang-Ho Moon, Byong-Tae Jeon, You‐Jin Jeon, Chang‐Bum Ahn, Jae‐Young Je, Pyo‐Jam Park,

Meat and Animal Product Quality

An angiotensin I-converting enzyme (ACE) inhibitory peptide was isolated and identified from hydrolysates of duck skin byproducts. Duck skin byproducts were hydrolyzed using nine proteases (Alcalase, Collagenase, Flavourzyme, Neutrase, papain, pepsin, Protamex, trypsin, and α-chymotrypsin) to produce an antihypertensive peptide. Of the various hydrolysates produced, the α-chymotrypsin hydrolysate exhibited the highest ACE inhibitory activity. The hydrolysate was purified using fast protein liquid chromatography (FPLC) and high-performance liquid chromatography (HPLC). The amino acid sequence of the ACE inhibitory peptide was identified as a hexapeptide Trp-Tyr-Pro-Ala-Ala-Pro, with a molecular weight of 693.90 Da. The peptide had an IC50 value of 137 μM, and the inhibitory pattern of the purified ACE inhibitor from duck skin byproducts was determined to be competitive by Lineweaver-Burk plots. In addition, the peptide was synthesized and the ACE inhibitory activity was verified in vivo. Spontaneously hypertensive rats (SHR) exhibited significantly decreased blood pressure and heart rate after peptide injection. Taken together, the results suggest that Trp-Tyr-Pro-Ala-Ala-Pro may be useful as a new antihypertensive agent.