Optimisation and validation of an angiotensin-converting enzyme inhibition assay for the screening of bioactive peptides

Vermeirssen, Vanessa; Camp, John Van; Verstraete, Willy

doi:10.1016/s0165-022x(02)00006-4

Cited by 202 publications

(139 citation statements)

References 30 publications

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“…In the literature, inconsiderable ACE inhibitory activities were reported for commercial soybean protein isolate (Lo & Li-Chan, 2005), flaxseed meal protein isolate (Marambe, Shand, & Wanasundara, 2008) and pumpkin meal protein isolate (Vastag, Popovic, Popovic, Krimer, & Pericin, 2011) unless they were hydrolyzed by proteases. The ACE inhibitory potential of hazelnut protein extracts was also higher than that of protease digested pea protein isolate (1.36 mg/mL) and comparable with that of protease digested whey protein isolate (0.90 mg/mL) (Vermeirssen, Van Camp, & Verstraete, 2002).…”

Section: Antihypertensive Activity Of Isolated Proteinsmentioning

confidence: 68%

Bioactive, functional and edible film-forming properties of isolated hazelnut (Corylus avellana L.) meal proteins

et al. 2014

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a b s t r a c tThis study aimed characterization of bioactive, functional and edible film making properties of isolated proteins from untreated (HPI), hot extracted (HPI-H), acetone washed (HPI-AW), and acetone washed and hot extracted (HPC-AW-H) hazelnut meals. The most bioactive protein extract was HPC-AW-H, followed by HPI-AW, HPI-H and HPI, based on antioxidant activity (TEAC and ORAC: 158 e461 mmol Trolox/kg), iron chelation (60.7e126.7 mmol EDTA/kg), angiotensin-converting enzyme inhibition (IC 50 : 0.57e1.0 mg/mL) and antiproliferative activity on colon cancer cells (IC 50 : 3.0e4.6 mg/ ml). Protein contents of HPI, HPI-H and HPI-AW (93.3e94.5%) were higher than that of HPC-AW-H (86.0%), but HPC-AW-H showed the best pH-solubility profile. The extracts showed good oil absorption (7.4e9.4 g/g) and foaming, but limited water holding and gelling capacities, and emulsion stability. The protein extracts gave transparent, yellowish to brownish and reddish colored and water soluble edible films. The HPI gave the lightest colored films with acceptable mechanical properties (elongation up to 144% and tensile strength up to 4.9 MPa). 1-D and 2-D electrophoresis clearly showed the molecular and isoelectric profiles of hazelnut proteins. The overall results of this study showed that the bioactive, solubility and gelation properties of hazelnut proteins could be improved by simple processes like acetone washing and/or heat treatment. The hazelnut proteins are valuable as multipurpose food ingredients.

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Section: Antihypertensive Activity Of Isolated Proteinsmentioning

confidence: 68%

Bioactive, functional and edible film-forming properties of isolated hazelnut (Corylus avellana L.) meal proteins

et al. 2014

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“…All the evaluated P. lunatus protein hydrolysates, those from Alcalase (R) or pepsin-pancreatin hydrolysis, exhibited ACE (Kim et al, 2004); same value for chickpea legumin (Yust et al, 2003); 1360 µg/mL for chickpea total protein (Vermeirssen et al, 2002); 300-1200 µg/mL for buck-wheat protein (Li et al, 2002) and 640 g/mL for mungo bean protein (Li et al, 2005). The IC 50 values reported for hydrolysates from animal protein sources differ noticeably: 8-11.2 μg/mL for milk protein (Gobbetti et al, 2000) and 20-74.4 μg/mL for egg white protein (Miguel et al, 2007).…”

Section: Ace Inhibitory Activity Of Protein Hydrolysates From P Lunatusmentioning

confidence: 97%

ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins

Magaña¹,

Campos²,

Dávila-Ortíz³

et al. 2015

Food Sci. Technol (Campinas)

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Phaseolus lunatus protein concentrates and the proteases Alcalase (R) and Pepsin-Pancreatin were used for the production of protein hydrolysates that inhibit angiotensin-I converting enzyme (ACE). Protein concentrate obtained from germinated and ungerminated seeds flour was hydrolyzed with Alcalase (R) at enzyme/substrate ratio (E/S) 1/10 and during 0.5 and 2.0 h, respectively. Dn the other hand, protein concentrate obtained from ungerminated (E/S: 1/10) and germinated (E/S: 1/50) seeds flour was sequentially hydrolyzed with Pepsin-Pancreatin during 1.0 and 3.0 h, respectively. Peptide fractions with ACE inhibitory activity in a range of 0.9 to 3.8 µg/mL were obtained by G-50 gel filtration chromatography and high-performance liquid chromatography C18 reverse phase chromatography. The observed amino acid composition suggests a substantial contribution of hydrophobic residues to the peptides' inhibitory potency, which potentially acts via blocking of angiotensin II production. These results show that P. lunatus seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with Alcalase (R) and Pepsin-Pancreatin.Keywords: P. lunatus; hydrolysates; peptides; ACE inhibitory activity.Practical Application: Legume proteins can enzymatically produce bioactive specific peptides for use in functional foods.

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“…The pH of the supernatant was adjusted to 8.3 and 20 µL of the filtrate was added to an aliquot of 200 µL hippurylhistidyl-leucine (Sigma) dissolved in sodium borate buffer of pH 8.5. Aliquot of 60 µL of the buffer was added to the mixture to maintain the pH of the reaction solution in the range between 8.1 and 8.3 [49]. The reaction was initiated by adding 20 µL of ACE solution followed by incubation at 37°C for 30 min.…”

Section: In Vitro Inhibition Of Angiotensin I-converting Enzyme (Ace mentioning

confidence: 99%

Proteolytic activity of dairy lactic acid bacteria and probiotics as determinant of growth and in vitro angiotensin-converting enzyme inhibitory activity in fermented milk

Donkor

Henriksson²,

Vasiljevic

et al. 2007

Lait

151

101

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-Two strains each of Lactobacillus acidophilus (L10 and La 4962), Bifidobacterium spp. (B. lactis B94 and B. longum Bl 536), and Lactobacillus casei (L26 and Lc 279), and one strain each of Streptococcus thermophilus (St 1342) and Lactobacillus delbrueckii ssp. bulgaricus (Lb 1466) were assessed for growth characteristics, proteolytic activity and release of in vitro angiotensin-converting enzyme inhibitory peptides in reconstituted skim milk. Single cultures grew well with exception of Lactobacillus delbrueckii ssp. bulgaricus. Despite slow growth, this culture produced substantial amount of lactic acid, second to S. thermophilus. All strains exhibited proteolytic activities with intra-and extracellular specific peptidases including X-prolyl-dipeptidyl aminopeptidase.

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Optimisation and validation of an angiotensin-converting enzyme inhibition assay for the screening of bioactive peptides

Cited by 202 publications

References 30 publications

Bioactive, functional and edible film-forming properties of isolated hazelnut (Corylus avellana L.) meal proteins

Bioactive, functional and edible film-forming properties of isolated hazelnut (Corylus avellana L.) meal proteins

ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins

Proteolytic activity of dairy lactic acid bacteria and probiotics as determinant of growth and in vitro angiotensin-converting enzyme inhibitory activity in fermented milk

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