The Impact of Germination and In Vitro Digestion on the Formation of Angiotensin Converting Enzyme (ACE) Inhibitory Peptides from Lentil Proteins Compared to Whey Proteins
نویسندگان
چکیده
Biologically active peptides are of particular interest in food science and human nutrition because they have been shown to play several physiological roles. In vitro gastrointestinal digestion of lentil and whey proteins in this study produced high angiotensin-I converting enzyme inhibitory activity with 75.5±1.9 and 91.4±2.3% inhibition, respectively. High ACE inhibitory activity was observed in lentil after 5 days of germination (84.3±1.2%). Fractionation by reverse phase chromatography gave inhibitory activities as high as 86.3±2.0 for lentil, 94.8±1.8% for whey and 93.7±1.7% at 5 day of germination. Further purification by HPLC resulted in several inhibitory peptides with IC50 values ranging from 0.064 to 0.164 mg/ml. These results demonstrate that lentil proteins are a good source of peptides with ACE inhibitory activity that can be released by germination or gastrointestinal digestion. Despite the lower bioactivity in comparison with whey proteins, incorporation of lentil proteins in functional food formulations and natural drugs look promising. Keywords—ACE inhibitory peptides, digestion, germination, lentil proteins, whey proteins.
منابع مشابه
High-pressure improves enzymatic proteolysis and the release of peptides with angiotensin I converting enzyme inhibitory and antioxidant activities from lentil proteins Running title: HP promotes the release of bioactive peptides from lentil proteins
*Manuscript Click here to view linked References 2 ABSTRACT 1 Angiotensin I converting enzyme (ACE) inhibitory and antioxidant peptides are receiving attention 2 due to their beneficial effects in the prevention/treatment of hypertension. The objective was to 3 explore the effect of high hydrostatic pressure (HP) on proteolysis by different proteases and the 4 release of bioactive peptides from...
متن کاملNovel angiotensin-converting enzyme inhibitory peptides from caseins and whey proteins of goat milk
Angiotensin-converting enzyme (ACE) plays a central role in blood pressure regulation by producing the vasoconstrictor angiotensin II. The inhibition of ACE with natural inhibitors, as alternatives to avoid the side effect of synthetic drugs, is a major target in the prevention of hypertension. In this study, we examined the separated caseins and whey proteins of goat milk for the presence of A...
متن کاملShort communication: bovine kappa-casein variants result in different angiotensin I converting enzyme (ACE) inhibitory peptides.
Proteins in bovine milk are a common source of bioactive peptides. The peptides are released by the digestion of caseins and whey proteins. Peptides derived from the different genetic variants A, B, C, E, F1, F2, G1, G2, H, I, and J of bovine kappa-casein (CSN3) were investigated for their inhibitory activities against angiotensin I converting enzyme (ACE). Amino acid sequences of the CSN3 vari...
متن کاملAngiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes
The objectives of the present study were two-fold: first, to detect whether salmon protein fractions possess angiotensin I-converting enzyme (ACE) inhibitory properties and whether salmon proteins can release ACE inhibitory peptides during a sequential in vitro hydrolysis (with commercial porcine enzymes) and ex vivo digestion (with human gastrointestinal enzymes). Secondly, to evaluate the ACE...
متن کاملNovel whey-derived peptides with inhibitory effect against angiotensin-converting enzyme: in vitro effect and stability to gastrointestinal enzymes.
Whey protein concentrate (WPC) was subjected to enzymatic hydrolysis by proteases from the flowers of Cynara cardunculus, and the resulting angiotensin-converting enzyme (ACE)-inhibitory effect was monitored. The whole WPC hydrolysate exhibited an IC(50) value of 52.9 ± 2.9 μg/mL, whereas the associated peptide fraction with molecular weight below 3 kDa scored 23.6 ± 1.1 μg/mL. The latter fract...
متن کامل