Angiotensin I converting enzyme inhibitory peptides from in vitro pepsin-pancreatin digestion of soy protein.
Angiotensin I converting enzyme (ACE) inhibitory activity was determined in the soy protein isolate (SPI) digest produced by in vitro pepsin-pancreatin sequential digestion. The inhibitory activity was highest within the first 20 min of pepsin digestion and decreased upon subsequent digestion with pancreatin. An IC(50) value of 0.28 +/- 0.04 mg/mL was determined after 180 min of digestion, while no ACE inhibitory activity was measured for the undigested SPI at 0.73 mg/mL. Chromatographic fractionation of the SPI digest resulted in IC(50) values of active fractions ranging from 0.13 +/- 0.03 to 0.93 +/- 0.08 mg/mL. Although many of the fractions showed ACE inhibition, peptides with lower molecular masses and higher hydrophobicities were most active. The findings show that many different peptides with ACE inhibitory activities were produced after in vitro pepsin-pancreatin digestion of SPI and lead to the speculation that physiological gastrointestinal digestion could also yield ACE inhibitory peptides from SPI.
Lo
Wendy M Y
WM
The University of British Columbia, Faculty of Agricultural Sciences, Food Science Building, 6650 N.W. Marine Drive, Vancouver, British Columbia V6T 1Z4, Canada.
Li-Chan
Eunice C Y
EC
D000596:Amino Acids / Q000032:analysis; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000032:analysis* / Q000737:chemistry / Q000494:pharmacology; D005591:Chemical Fractionation; D002851:Chromatography, High Pressure Liquid; D006868:Hydrolysis; D008970:Molecular Weight; D010194:Pancreatin / Q000378:metabolism*; D010434:Pepsin A / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis* / Q000494:pharmacology; D030262:Soybean Proteins / Q000737:chemistry / Q000378:metabolism*
D000596:Amino Acids; D000806:Angiotensin-Converting Enzyme Inhibitors; D010446:Peptide Fragments; D030262:Soybean Proteins; D010194:Pancreatin; D010434:Pepsin A