Evidence map›Paper›PMID 37761207›Full record

ArticleFoods (Basel, Switzerland)2023

Peptidomics Analysis of Soy Protein Hydrolysates-Antioxidant Properties and Mechanism of their Inhibition of the Oxidation of Palm Olein during Frying Cycles.

Annick Arcelle Pougoue Ngueukam, Mathilde Julie Klang, Ronice Zokou, Gires Teboukeu Boungo, Fabrice Djikeng Tonfack, Barakat Koyinsola Azeez, Hilaire Macaire Womeni, Apollinaire Tsopmo

Open access · goldAbstract read
In one paragraph

Article in Foods (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.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 29% 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, 4 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
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

8 authors at 2 institutions in 2 countries.

Annick Arcelle Pougoue NgueukamBiochemistry, Food Sciences, Nutrition and Medicinal Plants Research Unit, Department of Biochemistry, Faculty of Science, University of Dschang, Dschang P.O. Box 6, Cameroon.
Mathilde Julie KlangBiochemistry, Food Sciences, Nutrition and Medicinal Plants Research Unit, Department of Biochemistry, Faculty of Science, University of Dschang, Dschang P.O. Box 6, Cameroon.ORCID 0000-0002-8939-7846
Ronice ZokouBiochemistry, Food Sciences, Nutrition and Medicinal Plants Research Unit, Department of Biochemistry, Faculty of Science, University of Dschang, Dschang P.O. Box 6, Cameroon.ORCID 0000-0002-1117-997X
Gires Teboukeu BoungoBiochemistry, Food Sciences, Nutrition and Medicinal Plants Research Unit, Department of Biochemistry, Faculty of Science, University of Dschang, Dschang P.O. Box 6, Cameroon.
Fabrice Djikeng TonfackBiochemistry, Food Sciences, Nutrition and Medicinal Plants Research Unit, Department of Biochemistry, Faculty of Science, University of Dschang, Dschang P.O. Box 6, Cameroon.
Barakat Koyinsola AzeezFood Science Program, Department of Chemistry, Institute of Biochemistry, Carleton University, 1125 Colonel by Drive, Ottawa, ON K1S 5B6, Canada.
Hilaire Macaire WomeniBiochemistry, Food Sciences, Nutrition and Medicinal Plants Research Unit, Department of Biochemistry, Faculty of Science, University of Dschang, Dschang P.O. Box 6, Cameroon.
Apollinaire TsopmoFood Science Program, Department of Chemistry, Institute of Biochemistry, Carleton University, 1125 Colonel by Drive, Ottawa, ON K1S 5B6, Canada.ORCID 0000-0002-7062-0833
Université de Dschang · CMCarleton University · CA

Funding

Natural Sciences and Engineering Research Council of Canada 371908
6 · The paper itself

Abstract

This study determined for the first time the structure of the peptides (i.e., peptidomics) in soy protein hydrolysates and elucidated their effects on an oil's oxidative stability during frying cycles. The oil investigated was palm olein during 0, 4, 8, and 12 frying cycles of plantain banana chips. Proteins were extracted and hydrolyzed with two proteases. Trypsin hydrolysate (HTRY) exhibited higher anti-radical activity (DPPH, 70.2%) than the control (unhydrolyzed proteins, 33.49%) and pepsin hydrolysate (HPEP, 46.1%) at 200 µg/mL. HPEP however showed a 4.6-fold greater reduction of ferric ions (FRAP) while also possessing a higher peroxyl radical scavenging ability (716 ± 30 µM Trolox Eq/g) than HTRY (38.5 ± 35 µM Trolox Eq/g). During oil oxidative stability tests, HPEP improved the oxidative stability of the palm olein oil after 8 and 12 frying cycles, characterized by lower concentrations of hydroperoxides, and carbonyl and volatile compounds. HTRY however exerteda pro-oxidant activity. Structural data from SDS-PAGE and tandem mass spectrometry showed that the mechanism for the greater activity of the pepsin hydrolysate occurred due to unique structural features and a higher percentage of short-chain peptides. This was justified by a 25, 31, and 48% higher contents of tryptophan, histidine, and methionine, respectively (important amino acids with hydrogen atom transfer and electron-donating capacities) in the peptides identified in the pepsin hydrolysate.

Indexed as

antioxidantscarbonylsfrying cyclesmalondialdehydeoxidationpalm oleinpeptidomicsprotein hydrolysates

Identifiers

PMID37761207
PMCPMC10528889
OpenAlexW4386933459

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.