Evidence mapPaperPMID 37896038Full record

ArticlePlants (Basel, Switzerland)2023

Antioxidant Properties and Prediction of Bioactive Peptides Produced from Flixweed (sophia,

Na Thi Ty Ngo, Tharindu R L Senadheera, Fereidoon Shahidi

Open access · goldAbstract read
In one paragraph

Article in Plants (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 11% of its field
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

4 citing papers in PubMed, 1 synthesis or guideline pooled it, 15 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. 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 at 1 institution in 1 country.

Na Thi Ty NgoDepartment of Biochemistry, Memorial University of Newfoundland, St. John's, NL A1C 5S7, Canada.
Tharindu R L SenadheeraDepartment of Biochemistry, Memorial University of Newfoundland, St. John's, NL A1C 5S7, Canada.ORCID 0000-0002-3709-3541
Fereidoon ShahidiDepartment of Biochemistry, Memorial University of Newfoundland, St. John's, NL A1C 5S7, Canada.ORCID 0000-0002-9912-0330
Memorial University of Newfoundland · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flixweed (sophia) seed meal and camelina, both by-products of oil processing, were employed to generate protein hydrolysates by applying Flavourzyme and Alcalase. This study aimed to integrate in vitro and in silico methods to analyze sophia and camelina protein hydrolysates for releasing potent antioxidative, dipeptidyl peptidase IV (DPP IV) inhibitors and angiotensin-converting enzyme (ACE) inhibitory peptides. In vitro methods were used to investigate the antioxidant potential of sophia/camelina protein hydrolysates. Bioinformatics techniques, including Peptideranker, BIOPEP, Toxinpred, AlgPred, and SwissADME, were employed to obtain the identification of bioactive peptides produced during the hydrolysis process. Protein hydrolysates produced from sophia and camelina seed meal exhibited higher ABTS and DPPH radical scavenging activities Ithan their protein isolates. Among the produced protein hydrolysates, Alcalase-treated samples showed the highest oxygen radical absorbance capacity and hydroxyl radical scavenging activity. In addition, sophia/camelina hydrolysates prevented hydroxyl and peroxyl radical-induced DNA scission and LDL cholesterol oxidation. In silico proteolysis was conducted on Alcalase-treated samples, and resultant peptides showed potential DPP IV and ACE-inhibitory activities. Identified peptides were further assessed for their toxicity and medicinal properties. Results indicate that all digestive-resistant peptides were non-toxic and had desirable drug-like properties. The findings of this study suggest that sophia/camelina protein hydrolysates are promising candidates for functional foods, nutraceuticals, and natural therapeutics.

Indexed as

angiotensin-converting enzyme (ACE) inhibitory peptidesantioxidant activitybioactive peptidesbioinformaticsBIOPEP-UWM databasedipeptidyl peptidase IV (DPP IV) inhibitory peptide

Identifiers

PMID37896038
PMCPMC10609683
OpenAlexW4387639055

What Socratic 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 Socratic graph.