Storage stability of the synthetic angiotensin converting enzyme (ACE) inhibitory peptides separated from beef sareoplasmic protein extracts at different pH, temperature, and gastric digestion

Abstract

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 peptides was measured after 2 months of storage at 4 degrees 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 degrees 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.