Identification and quantification of ACE-inhibiting peptides in enzymatic hydrolysates of plant proteins.

Steffi Rudolph, Diana Lunow, Susanne Kaiser, Thomas Henle

Food chemistry 2017 Jun 01

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Enzymatic hydrolysis of proteins from rice, soy, pea and wheat, with both chymotrypsin and thermolysin, resulted in hydrolysates, which are efficient inhibitors of the angiotensin-converting enzyme (ACE). IC50 values of the hydrolysates were between 27 and 39mg/l, which is comparable to enzymatically hydrolysed whey protein. A significant increase of the ACE-inhibiting effect was observed following butanol extraction due to accumulation of hydrophobic peptides (IC50 between 12 and 21mg/l). Based on the identification and quantification of individual tryptophan-, tyrosine- and phenylalanine-containing dipeptides, 50-80% of the total ACE-inhibiting potential of butanol extracts from plant protein hydrolysates could be explained. Compared to hydrolysates from whey protein, where the inhibitory effect can almost exclusively be attributed to Ile-Trp, the ACE inhibition by plant protein hydrolysates is caused by a variety of peptides, in particular tyrosine-containing peptides. Hydrolysates of plant proteins are promising ingredients for the development of functional foods. Copyright © 2016. Published by Elsevier Ltd.

Citation

Steffi Rudolph, Diana Lunow, Susanne Kaiser, Thomas Henle. Identification and quantification of ACE-inhibiting peptides in enzymatic hydrolysates of plant proteins. Food chemistry. 2017 Jun 01;224:19-25