ArticleBioMed research international2014
Angiotensin I converting enzyme inhibitory peptides obtained after in vitro hydrolysis of pea (Pisum sativum var. Bajka) globulins.
Article in BioMed research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 58 citations in OpenAlex.
- Pulse protein quality and derived bioactive peptides.Frontiers in plant science · 2025Review
- Identification of New Angiotensin-Converting Enzyme Inhibitory Peptides Isolated from the Hydrolysate of the Venom ofToxins · 2024Article
- A Comprehensive Review of Pea (Foods (Basel, Switzerland) · 2023Review
- Recent Advances in In Vitro and In Vivo Studies of Antioxidant, ACE-Inhibitory and Anti-Inflammatory Peptides from Legume Protein Hydrolysates.Molecules (Basel, Switzerland) · 2023Review
- Significance of whey protein hydrolysate on anti-oxidative, ACE-inhibitory and anti-inflammatory activities and release of peptides with biofunctionality: an in vitro and in silico approach.Journal of food science and technology · 2022Article
- Health Benefits of Cereal Grain- and Pulse-Derived Proteins.Molecules (Basel, Switzerland) · 2022Review
- Peptidomic profiling of fermented goat milk: considering the fermentation-time dependent proteolysis byJournal of food science and technology · 2022Article
- A Novel Angiotensin-I-Converting Enzyme (ACE) Inhibitory Peptide fromMarine drugs · 2021Article
- The Effect ofPlants (Basel, Switzerland) · 2021Article
- Characterisation of Biologically Active Hydrolysates and Peptide Fractions of Vacuum Packaging String Bean (Foods (Basel, Switzerland) · 2020Article
- A Pea (Foods (Basel, Switzerland) · 2020Article
- Characteristics of New Peptides GQLGEHGGAGMG, GEHGGAGMGGGQFQPV, EQGFLPGPEESGR, RLARAGLAQ, YGNPVGGVGH, and GNPVGGVGHGTTGT as Inhibitors of Enzymes Involved in Metabolic Syndrome and Antimicrobial Potential.Molecules (Basel, Switzerland) · 2020Article
- The Inhibition of Amylase and ACE Enzyme and the Reduction of Immunoreactivity of Sourdough Bread.Foods (Basel, Switzerland) · 2020Article
- Different Temperature Treatments of Millet Grains Affect the Biological Activity of Protein Hydrolyzates and Peptide Fractions.Nutrients · 2019Article
- Review
- Enhancement of yield, nutritional and nutraceutical properties of two common bean cultivars following the application of seaweed extract (Saudi journal of biological sciences · 2018Article
- Angiotensin-1-converting enzyme inhibition, antioxidant activity, and modulation of cerebral Na+/K+ ATPase by free phenolics of African locust bean (Parkia biglobosa).Health science reports · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pea seeds represent a valuable source of active compounds that may positively influence health. In this study, the pea globulins were digested in vitro under gastrointestinal condition and potentially bioaccessible angiotensin I converting enzyme (ACE) inhibitory peptides were identified. The degree of hydrolysis after pepsin, 14.42%, and pancreatin, 30.65%, were noted. The peptides with the highest ACE inhibitory properties were separated using ion exchange chromatography on DEAE-cellulose. Thirteen peptides fractions were obtained but only four showed potential antihypertensive properties. The highest inhibitory activity was determined for the fraction F8 (IC50 = 0.0014 mg/mL). This fraction was separated on Sephadex G10 and two peptide fractions were obtained. The peptides fraction (B) with the highest ACE inhibitory activity (IC50 = 0.073 mg/mL) was identified by ESI-MS/MS. The sequences of ACE inhibitory peptides were GGSGNY, DLKLP, GSSDNR, MRDLK, and HNTPSR. Based on Lineweaver-Burk plots for the fraction B, the kinetic parameters as K m, Vmax, and K i and mode of inhibition were determined. This fraction belongs to uncompetitive inhibitor of ACE activity. The seeds of pea are the source of precursor protein, which releases the ACE inhibitory peptides as a result of enzymatic hydrolysis.
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