• Food Science and Biotechnology
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• 제16권4호
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• pp.572-575
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• 2007

The angiontensin converting enzyme (ACE) inhibitory peptides were separated from beef sarcoplasmic protein extract and their amino acid sequences were identified as GFHI, DFHINQ, FHG, and GLSDGEWQ. The 4 peptides were synthesized in a laboratory and the ACE inhibitory activities of pep tides was measured after 2 months of storage at $4^{\circ}C$ under different pH conditions (6.0, 6.5, 7.0, 7.5, and 8.0) and the exposure of different temperatures (70, 80, 90, and $100^{\circ}C$) for 20 min to evaluate industrial use. No significant difference was detected by pH and temperature abuse for 20 min during storage. When the synthetic peptides were digested by pepsin, trypsin, and chymotrypsin, the ACE inhibitory activity was not changed. These results indicated that the 4 synthetic peptides with ACE inhibitory activity were pH-stable, heat-stable, and resistant to proteinases in gastro-intestinal tracts. Therefore, those 4 peptides can be used as a source for functional food product with various applications.