| Autor: |
Masomeh Ghassem, Mamot Said, Keizo Arihara, Abdul Salam Babji, Saadiah Ibrahim |
| Rok vydání: |
2011 |
| Předmět: |
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| Zdroj: |
Food Chemistry. 129:1770-1777 |
| ISSN: |
0308-8146 |
| DOI: |
10.1016/j.foodchem.2011.06.051 |
| Popis: |
Haruan myofibrillar protein was hydrolysed with proteinase K and thermolysin to isolate Angiotensin converting enzyme (ACE) inhibitory peptides. The thermolysin hydrolysate of myofibrillar protein with the highest ACE inhibition activity (IC 50 = 0.033 mg/ml) was fractionated by ultrafiltration and size exclusion chromatography to three fractions. Fraction F2 with higher ACE inhibitory activity was separated into five fractions (A–E) using reversed-phased high performance liquid chromatography (RP-HPLC). Fraction C showed 81% inhibition activity and was subjected to HPLC coupled to electrospray ionisation-time-of-flight mass spectrometry (ESI-TOF MS/MS). Two peptide sequences for the most abundant fragments were identified as VPAAPPK (IC 50 = 0.45 μM) at 791.155 m/z and NGTWFEPP (IC 50 = 0.63 μM) at 1085.841 m/z . The presence of two proline residues at the C-terminal sequence is responsible for the high ACE inhibitory activity of these peptides. The results suggest that Haruan meat protein hydrolysate is a potent ACE inhibitor and may be used to decrease blood pressure. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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Full Text from ScienceDirect