Cited by 137Protein Hydrolysis and Bioactive PeptidesRenin-Angiotensin System StudiesPeptidase Inhibition and Analysis

Structural and Antihypertensive Properties of Enzymatic Hemp Seed Protein Hydrolysates

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Malomo, Sunday, Onuh, John, Girgih, Abraham, Aluko, Rotimi·2015·Nutrients

Abstract

The aim of this work was to produce antihypertensive protein hydrolysates through different forms of enzymatic hydrolysis (2% pepsin, 4% pepsin, 1% alcalase, 2% alcalase, 2% papain, and 2% pepsin + pancreatin) of hemp seed proteins (HSP). The hemp seed protein hydrolysates (HPHs) were tested for in vitro inhibitions of renin and angiotensin-converting enzyme (ACE), two of the enzymes that regulate human blood pressure. The HPHs were then administered orally (200 mg/kg body weight) to spontaneously hypertensive rats and systolic blood pressure (SBP)-lowering effects measured over a 24 h period. Size exclusion chromatography mainly showed a 300–9560 Da peptide size range for the HPHs, while amino acid composition data had the 2% pepsin HPH with the highest cysteine content. Fluorescence spectroscopy revealed higher fluorescence intensities for the peptides when compared to the unhydrolyzed hemp seed protein. Overall, the 1% alcalase HPH was the most effective (p < 0.05) SBP-reducing agent (−32.5 ± 0.7 mmHg after 4 h), while the pepsin HPHs produced longer-lasting effects (−23.0 ± 1.4 mmHg after 24 h). We conclude that an optimized combination of the fast-acting HPH (1% alcalase) with the longer-lasting HPHs (2% and 4% pepsin) could provide daily effective SBP reductions.

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Authors
Malomo, S., Onuh, J., Girgih, A., & Aluko, R.
Affiliations
University of Manitoba (CA)
Corresponding author
Aluko, Rotimi
Venue
Nutrients
Publisher
MDPI AG
Published
2015-09-10
Volume
7
Issue
9
Pages
7616-7632
ISSN
2072-6643 (ISSN-L)
OpenAlex
W2120270466
Cited by
137
References
3
Citations by year
2026: 9 · 2025: 15 · 2024: 17 · 2023: 12 · 2022: 23 · 2021: 15 · 2020: 11 · 2019: 12 · 2018: 7 · 2017: 11 · 2016: 5
FWCI
3.33
Type
journal article
Language
en
Open access
Locations
  • Nutrients (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • University of Manitoba
  • Natural Sciences and Engineering Research Council of Canada
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Renin-Angiotensin System Studies
  • Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
Keywords
hemp seed protein, protein hydrolysates, enzymatic hydrolysis, antihypertensive peptides, renin inhibition, angiotensin-converting enzyme inhibition, pepsin, alcalase, papain, pancreatin, spontaneously hypertensive rats, systolic blood pressure, peptide size distribution, cysteine content
MeSH terms
Renin Inhibitors, Angiotensin-Converting Enzyme Inhibitors, Animals, Antihypertensive Agents, Blood Pressure, Cannabis, Chromatography, Gel, Disease Models, Animal, Hypertension, Male, Phytotherapy, Pepsin A, Plant Proteins, Plants, Medicinal, Protein Hydrolysates, Rats, Inbred SHR, Renin, Renin-Angiotensin System, Seeds, Spectrometry, Fluorescence, Subtilisins

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