Evidence mapPaperPMID 40560266Full record

ArticleBioprocess and biosystems engineering2025

Proteomics and bioinformatics guided discovery of microalgal multifunctional peptides for novel nutraceutical applications.

Montassar Romdhani, Jihen Dhaouafi, Barbara Deracinois, Christophe Flahaut, Naïma Nedjar, Rafik Balti

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In one paragraph

Article in Bioprocess and biosystems engineering, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

6 authors.

Montassar RomdhaniUMR Transfrontalière BioEcoAgro N°1158, Université Lille, INRAE, Université Liège, UPJV, YNCREA, Université Artois, Université Littoral Côte d'Opale, ICV-Institut Charles Viollette, F-59000, Lille, France.
Jihen DhaouafiUMR Transfrontalière BioEcoAgro N°1158, Université Lille, INRAE, Université Liège, UPJV, YNCREA, Université Artois, Université Littoral Côte d'Opale, ICV-Institut Charles Viollette, F-59000, Lille, France.
Barbara DeracinoisUMR Transfrontalière BioEcoAgro N°1158, Université Lille, INRAE, Université Liège, UPJV, YNCREA, Université Artois, Université Littoral Côte d'Opale, ICV-Institut Charles Viollette, F-59000, Lille, France.
Christophe FlahautUMR Transfrontalière BioEcoAgro N°1158, Université Lille, INRAE, Université Liège, UPJV, YNCREA, Université Artois, Université Littoral Côte d'Opale, ICV-Institut Charles Viollette, F-59000, Lille, France.
Naïma Nedjar *UMR Transfrontalière BioEcoAgro N°1158, Université Lille, INRAE, Université Liège, UPJV, YNCREA, Université Artois, Université Littoral Côte d'Opale, ICV-Institut Charles Viollette, F-59000, Lille, France.
Rafik Balti *Université Paris-Saclay, CentraleSupélec, Laboratoire de Génie des Procédés et Matériaux, Centre Européen de Biotechnologie et de Bioéconomie (CEBB), 3 Rue des Rouges Terres, 51110, Pomacle, France. rafik.balti@centralesupelec.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study aimed to identify and characterize bioactive peptides derived from protein hydrolysates of Arthrospira platensis (APPH) and Tetraselmis chuii (TCPH) using an integrated peptidomics and bioinformatics approach. Proteins extracted from the microalgae were hydrolyzed using pepsin (EC 3.4.23.1) at various enzyme/substrate (E/S) ratios. APPH and TCPH, prepared at an E/S ratio of 1/10 (w/w), were analyzed using peptidomics through reverse-phase high-performance liquid chromatography (RP-HPLC) coupled with tandem mass spectrometry (MS/MS). Using the UniProtKB database, a total of 265 unique peptides were identified, including 187 peptides from APPH and 78 peptides from TCPH. Subsequent in silico analysis of these peptides revealed favorable physicochemical properties, with a notable distribution of hydrophobic (APPH: 26; TCPH: 5), amphipathic (APPH: 70; TCPH: 16), and hydrophilic peptides (APPH: 59; TCPH: 17). Toxicity assessments confirmed that none of the peptides showed hemolytic or cytotoxic risks, except for one peptide identified in TCPH with potential cytotoxicity. Furthermore, bioactivity predictions demonstrated significant multifunctional properties (scores exceeding the 0.500 threshold), identifying peptides with antihypertensive (APPH: 2; TCPH: 1), anti-diabetic (APPH: 2), anti-inflammatory (APPH: 14; TCPH: 5) and antimicrobial (APPH: 7) activities. The current study thus establishes protein hydrolysates from A. platensis and T. chuii as promising sources of bioactive peptides suitable for nutraceutical applications. Our integrated analytical and computational strategy provides critical insights into peptide multifunctionality, supporting further research and development of microalgae-derived peptides.

Indexed as

Algal ProteinsComputational BiologyDietary SupplementsMicroalgaePeptidesProteomicsSpirulinaAnimalsProtein HydrolysatesAlgal ProteinsPeptidesProtein HydrolysatesBioactive peptidesEnzymatic hydrolysisIn silico analysisMicroalgaePeptidomics

Identifiers

What Socratic holds

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Registered trials

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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.