Soy Research Today is a free monthly online journal that collates and summarizes the latest research about Soy, including details on soy milk, soy protein, soya bean, benefits, dangers.

Angiotensin I converting enzyme inhibitory peptides from in vitro pepsin-pancreatin digestion of soy protein.

Lo WM, Li-Chan EC

The University of British Columbia, Faculty of Agricultural Sciences, Food Science Building, 6650 N.W. Marine Drive, Vancouver, British Columbia V6T 1Z4, Canada.

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.

Published 27 April 2005 in J Agric Food Chem, 53(9): 3369-76.
Full-text of this article is available online (may require subscription).

© 2004-2008 Soy Research Today. All Rights Reserved.