Structural and Antihypertensive Properties of Enzymatic Hemp Seed Protein Hydrolysates
Open accessAbstract
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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The ACE-inhibitory values of the biorefinery products are in the range of previous results on hemp seed protein hydrolysates.
“These values are in the range of previous results obtained on hemp seed protein hydrolysates.”
From Comparing the Effectiveness of Three Different Biorefinery Processes at Recovering Bioactive Products from Hemp (Cannabis sativa L.) Byproduct (2020) · cites this paper as Malomo et al. 2015
IC50 values from 16 to 228 mg/L were measured in hemp seed proteins treated by different enzymes.
“Besides, IC 50 values from 16 to 228 mg/L were measured in hemp seed proteins treated by different enzymes (Malomo et al. 2015).”
From Comparing the Effectiveness of Three Different Biorefinery Processes at Recovering Bioactive Products from Hemp (Cannabis sativa L.) Byproduct (2020) · cites this paper as Malomo et al. 2015
Many other studies have demonstrated that antihypertensive peptides with varying potencies can be generated simply by treating protein substrates with different enzymes and enzyme:substrate ratios.
“Many other studies have demonstrated that antihypertensive peptides with varying potencies can be generated simply by treating protein substrates with different enzymes and enzyme: substrate ratios (Rizzello et al. 2016; Malomo et al. 2015).”
From Comparing the Effectiveness of Three Different Biorefinery Processes at Recovering Bioactive Products from Hemp (Cannabis sativa L.) Byproduct (2020) · cites this paper as Malomo et al. 2015
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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)
- PMC
- PMC4586553
- 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
- gold
- dx.doi.org
- Licence
- 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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