Purification and identification of ACE inhibitory peptides from Haruan (Channa striatus) myofibrillar protein hydrolysate using HPLC–ESI-TOF MS/MS
作者： Masomeh Ghassem , Keizo Arihara , Abdul Salam Babji , Mamot Said , Saadiah Ibrahim
DOI: 10.1016/J.FOODCHEM.2011.06.051
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摘要: Abstract Haruan myofibrillar protein was hydrolysed with proteinase K and thermolysin to isolate Angiotensin converting enzyme (ACE) inhibitory peptides. The hydrolysate of the highest ACE inhibition activity (IC 50 = 0.033 mg/ml) fractionated by ultrafiltration size exclusion chromatography three fractions. Fraction F2 higher separated into five fractions (A–E) using reversed-phased high performance liquid (RP-HPLC). C showed 81% subjected HPLC coupled electrospray ionisation-time-of-flight mass spectrometry (ESI-TOF MS/MS). Two peptide sequences for most abundant fragments were identified as VPAAPPK = 0.45 μM) at 791.155 m/z NGTWFEPP = 0.63 μM) 1085.841 . presence two proline residues C-terminal sequence is responsible these results suggest that meat a potent inhibitor may be used decrease blood pressure.
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