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The Impact of Fermentation and In Vitro Digestion on the Formation of Angiotensin-I-Converting Enzyme Inhibitory Activity from Pea and Whey Protein

V. Vermeirssen^*,, J. Van Camp, K. Decroos^*, L. Van Wijmelbeke and W. Verstraete^*

^* Department of Biochemical and Microbial Technology
Department of Food Technology and Nutrition, Faculty of Agricultural and Applied Biological Sciences, Ghent University, 9000 Ghent, Belgium

Corresponding author:
W. Verstraete; e-mail:
willy.verstraete{at}rug.ac.be.

Pea and whey protein were fermented by Lactobacillus helveticusand Saccharomyces cerevisiae in monoculture and in combination at 28 and 37°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°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.

Key Words: ACE inhibitory peptide • fermentation • gastrointestinal digestion

Abbreviation key: ACE = angiotensin-I-converting enzyme, GRAS = generally recognized as safe, IC₅₀ = 50% inhibitory concentration, MWCO = molecular weight cut off, SHR = spontaneously hypertensive rats

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