Evidence map›Paper›PMID 38539879›Full record

ArticleAntioxidants (Basel, Switzerland)2024

Screening for Metal-Chelating Activity in Potato Protein Hydrolysates Using Surface Plasmon Resonance and Peptidomics.

Mads Bjørlie, Julie Christina Hartmann, Line Hyrup Rasmussen, Betül Yesiltas, Ann-Dorit Moltke Sørensen, Simon Gregersen Echers, Charlotte Jacobsen

Open access · goldAbstract read
In one paragraph

Article in Antioxidants (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
2.3field-weighted citation impact, top 12% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Mads BjørlieNational Food Institute, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark.
Julie Christina HartmannNational Food Institute, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark.
Line Hyrup RasmussenNational Food Institute, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark.
Betül YesiltasNational Food Institute, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark.ORCID 0000-0002-4587-9990
Ann-Dorit Moltke SørensenNational Food Institute, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark.ORCID 0000-0001-9349-1221
Simon Gregersen EchersDepartment of Chemistry and Bioscience, Aalborg University, 9220 Aalborg, Denmark.ORCID 0000-0001-9349-3235
Charlotte JacobsenNational Food Institute, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark.ORCID 0000-0003-3540-9669
Technical University of Denmark · DKAalborg University · DK

Funding

Partially funded by US company Kalsec N/A
6 · The paper itself

Abstract

Metal-catalyzed lipid oxidation is a major factor in food waste, as it reduces shelf life. Addressing this issue, our study investigates the potential of hydrolysates derived from potato protein, a by-product of potato starch production, as metal-chelating antioxidants. Through sequential enzymatic hydrolysis using alcalase or trypsin combined with Flavourzyme, we produced various hydrolysates, which were then fractionated using ultrafiltration. Using a combination of peptidomics and bioinformatics, we predicted the presence of metal-chelating and free radical-scavenging peptides across all hydrolysate fractions, with a trend indicating a higher content of antioxidant peptides in lower molecular weight fractions. To validate these predictions, we utilized surface plasmon resonance (SPR) and a 9-day emulsion storage experiment. While SPR demonstrated potential in identifying antioxidant activity, it faced challenges in differentiating between hydrolysate fractions due to significant standard errors. In the storage experiment, all hydrolysates showed lipid oxidation inhibition, though not as effectively as ethylenediaminetetraacetic acid (EDTA). Remarkably, one fraction (AF13) was not significantly different (

Indexed as

antioxidant peptidesbioinformaticsemulsionslipid oxidationmass spectrometryNi-NTA bindingsequential hydrolysis

Identifiers

PMID38539879
PMCPMC10968033
OpenAlexW4392763547

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.