Evidence map›Paper›PMID 39582575›Full record

ArticleCurrent research in food science2024

Ultrasonication coupled to enzymatic hydrolysis of soybean okara proteins for producing bioactive and bioavailable peptides.

Lorenza d'Adduzio, Melissa Fanzaga, Anna Laura Capriotti, Enrico Taglioni, Giovanna Boschin, Aldo Laganà, Lukas Rueller, Josef Robert, Antje van Gemmern, Carlotta Bollati and 1 more

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Article in Current research in food science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Seaweed (Journal of agricultural and food chemistry · 2025
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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

11 authors.

Lorenza d'AdduzioDepartment of Pharmaceutical Sciences, University of Milan, Via Mangiagalli 25, 20133, Milan, Italy.
Melissa FanzagaDepartment of Pharmaceutical Sciences, University of Milan, Via Mangiagalli 25, 20133, Milan, Italy.
Anna Laura CapriottiDepartment of Chemistry, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185, Rome, Italy.
Enrico TaglioniDepartment of Chemistry, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185, Rome, Italy.
Giovanna BoschinDepartment of Pharmaceutical Sciences, University of Milan, Via Mangiagalli 25, 20133, Milan, Italy.
Aldo LaganàDepartment of Chemistry, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185, Rome, Italy.
Lukas RuellerFraunhofer Institute for Environmental, Safety and Energy Technology UMSICHT, 46047, Oberhausen, Germany.
Josef RobertFraunhofer Institute for Environmental, Safety and Energy Technology UMSICHT, 46047, Oberhausen, Germany.
Antje van GemmernFraunhofer Institute for Environmental, Safety and Energy Technology UMSICHT, 46047, Oberhausen, Germany.
Carlotta BollatiDepartment of Pharmaceutical Sciences, University of Milan, Via Mangiagalli 25, 20133, Milan, Italy.
Carmen LammiDepartment of Pharmaceutical Sciences, University of Milan, Via Mangiagalli 25, 20133, Milan, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This work was aimed to explore the antioxidative properties, bioavailability and the safety of bioactive peptides obtained by the enzymatic hydrolysis of ultrasound-treated (UO) and untreated (nUO) soybean okara proteins. Particularly, the peptidomic profiles of both hydrolysates were examined using an untargeted metabolomics technique for suspect screening that was specifically designed for the profiling of short-chain peptides and relied on ultra-high-performance liquid chromatography coupled to high-resolution mass spectrometry (UHPLC-HRMS) and bioinformatics. Next, both UO and nUO hydrolysates reduce Dipeptidyl peptidase-IV (DPP-IV) enzyme activity until 39.54 ± 0.26 % and 43.29 ± 0.36 % respectively and inhibit angiotensin converting enzyme (ACE) activities by 30.54 ± 0.42 % and 30.76 ± 0.02 %, respectively. Moreover, they demonstrate to exerted antioxidant properties. Particularly, they show a comparable

Indexed as

Angiotensin-converting enzyme (ACE)Antioxidant activityBioactive peptidesDipeptidyl peptidase-IV (DPP-IV)OkaraPeptide bioavailabilitySoybean okara

Identifiers

PMID39582575
PMCPMC11582538

What Socratic holds

Textmetadata
LicenceCC BY
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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.