title: The impact of fermentation and in vitro digestion on the formation of angiotensin-I-converting enzyme inhibitory activity from pea and whey protein.
abstract: Pea and whey protein were fermented by Lactobacillus helveticus and Saccharomyces cerevisiae in monoculture and in combination at 28 and 37 degrees C in order to release angiotensin-I-converting enzyme (ACE) inhibitory peptides. The fermentation products were subjected to in vitro gastrointestinal digestion, and the digests of nonfermented samples served as controls. After fermentation, the ACE inhibitory activity (%) increased by 18 to 30% for all treatments, except for the fermentations of whey protein with Saccharomyces cerevisiae at 28 degrees C, where no significant change was observed. After digestion, however, both fermented and nonfermented samples reached maximum ACE inhibitory activity. The whey digests tended to have lower (50%) inhibitory concentrations (IC50; 0.14 to 0.07 mg/ml), hence, higher ACE inhibitory activity, than the pea digests (0.23 to 0.11 mg/ml). The nonfermented whey protein digest showed the highest ACE inhibitory activity of all. For pea protein, the nonfermented sample had the lowest IC50 value. These results suggest that in vitro gastrointestinal digestion was the predominant factor controlling the formation of ACE inhibitory activity, hence, indicating its importance in the bioavailability of ACE inhibitory peptides.
authors.affiliation: Department of Biochemical and Microbial Technology, Faculty of Agricultural and Applied Biological Sciences, Ghent University, 9000 Ghent, Belgium.
authors.forename: V
authors.initials: V
authors.lastname: Vermeirssen
authors.forename: J
authors.initials: J
authors.lastname: Van Camp
authors.forename: K
authors.initials: K
authors.lastname: Decroos
authors.forename: L
authors.initials: L
authors.lastname: Van Wijmelbeke
authors.forename: W
authors.initials: W
authors.lastname: Verstraete
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000032:analysis* / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000378:metabolism; D004063:Digestion; D010450:Endopeptidases / Q000378:metabolism; D005285:Fermentation; D007778:Lactobacillus / Q000378:metabolism; D008894:Milk Proteins / Q000737:chemistry*; D018532:Pisum sativum / Q000737:chemistry*; D010434:Pepsin A / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism; D000067816:Whey Proteins
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D008894:Milk Proteins; D010940:Plant Proteins; D000067816:Whey Proteins; D010450:Endopeptidases; D002918:Chymotrypsin; C117608:alpha-chymotrypsin; D014357:Trypsin; D010434:Pepsin A