Identification and quantification of ACE-inhibiting peptides in enzymatic hydrolysates of plant proteins
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
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 39 mg/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 21 mg/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. (C) 2016 Published by Elsevier Ltd.
Details
Original language | English |
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Pages (from-to) | 19-25 |
Number of pages | 7 |
Journal | Food Chemistry |
Volume | 224 |
Publication status | Published - 1 Jun 2017 |
Peer-reviewed | Yes |
External IDs
Scopus | 85006959913 |
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WOS | 000394631400003 |
Keywords
Keywords
- Angiotensin-converting enzyme (ACE), Bioactive peptides, Plant proteins, Hydrolysate, Tryptophan-, tyrosine and phenylalanine-containing dipeptides, Functional food, I-CONVERTING-ENZYME, SPONTANEOUSLY HYPERTENSIVE-RATS, TRYPTOPHAN-CONTAINING DIPEPTIDES, RANDOMIZED CONTROLLED-TRIAL, ANGIOTENSIN-I, BLOOD-PRESSURE, SELECTIVE INHIBITORS, UNDARIA-PINNATIFIDA, BIOACTIVE PEPTIDES, ACTIVE-SITES