Evidence map›Paper›PMID 38275690›Full record

ArticleFoods (Basel, Switzerland)2024

Enzymatic Hydrolysis of Water Lentil (Duckweed): An Emerging Source of Proteins for the Production of Antihypertensive Fractions.

Marie-Ève Bernier, Jacinthe Thibodeau, Laurent Bazinet

Abstract read
In one paragraph

Article in Foods (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed.

  1. Review
  2. Article
  3. Foods (Basel, Switzerland) · 2026
    Review
  4. Review
  5. Novel Angiotensin-Converting Enzyme Inhibitory Peptides fromPharmaceuticals (Basel, Switzerland) · 2026
    Article
  6. Review
  7. Review
  8. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Marie-Ève BernierDepartment of Food Sciences, Laboratoire de Transformation Alimentaire et Procédés ÉlectroMembranaires (LTAPEM, Laboratory of Food Processing and ElectroMembrane Processes), Institute of Nutrition and Functional Foods (INAF), Université Laval, Quebec, QC G1V 0A6, Canada.
Jacinthe ThibodeauDepartment of Food Sciences, Laboratoire de Transformation Alimentaire et Procédés ÉlectroMembranaires (LTAPEM, Laboratory of Food Processing and ElectroMembrane Processes), Institute of Nutrition and Functional Foods (INAF), Université Laval, Quebec, QC G1V 0A6, Canada.
Laurent BazinetDepartment of Food Sciences, Laboratoire de Transformation Alimentaire et Procédés ÉlectroMembranaires (LTAPEM, Laboratory of Food Processing and ElectroMembrane Processes), Institute of Nutrition and Functional Foods (INAF), Université Laval, Quebec, QC G1V 0A6, Canada.ORCID 0000-0002-6818-3558

Funding

Fonds de recherche du Québec -Nature et technologies (FRQ-NT) 319488NSERC, Alliance Grant: "Integrated valorization of coproducts by ecoefficient food technologies in the context of a circular economy (Consortium VITALE)" ALLRP561008-20
6 · The paper itself

Abstract

Water lentil (Duckweed), an emerging protein source, is a small floating aquatic plant with agronomic and compositional characteristics rendering it a potential source of bioactive peptides. However, enzymatic hydrolysis of duckweeds has only been carried out to assess the antioxidant and antimicrobial activities of the hydrolysates. The main objectives of this study were to perform enzymatic hydrolysis of duckweed powder utilizing several enzymes and to evaluate the final antihypertensive activity of the fractions. Duckweed powder was efficiently hydrolyzed by pepsin, chymotrypsin, papain and trypsin, with degree of hydrolysis ranging from 3% to 9%, even without prior extraction and concentration of proteins. A total of 485 peptide sequences were identified in the hydrolysates and only 51 were common to two or three hydrolysates. It appeared that phenolic compounds were released through enzymatic hydrolyses and primarily found in the supernatants after centrifugation at concentrations up to 11 mg gallic acid/g sample. The chymotryptic final hydrolysate, the chymotryptic supernatant and the papain supernatant increased the ACE inhibitory activity by more than 6- to 8-folds, resulting in IC

Indexed as

ACE-inhibitorbioactive peptideduckweedenzymatic hydrolysistotal phenolic content

Identifiers

PMID38275690
PMCPMC10814938

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.