Evidence map›Paper›PMID 37685861›Full record

ArticleInternational journal of molecular sciences2023

Comparison of the Bioactive Properties of Human and Bovine Hemoglobin Hydrolysates Obtained by Enzymatic Hydrolysis: Antimicrobial and Antioxidant Potential of the Active Peptide α137-141.

Ahlam Outman, Barbara Deracinois, Christophe Flahaut, Mira Abou Diab, Jihen Dhaouefi, Bernard Gressier, Bruno Eto, Naïma Nedjar

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. 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

8 authors.

Ahlam OutmanUMR Transfrontalière BioEcoAgro N_1158, Institut Charles Viollette, National Research Institute for Agriculture, Food and the Environment, Université Lille, F-59000 Lille, France.
Barbara DeracinoisUMR Transfrontalière BioEcoAgro N_1158, Institut Charles Viollette, National Research Institute for Agriculture, Food and the Environment, Université Lille, F-59000 Lille, France.ORCID 0000-0002-0279-2449
Christophe FlahautUMR Transfrontalière BioEcoAgro N_1158, Institut Charles Viollette, National Research Institute for Agriculture, Food and the Environment, Université Lille, F-59000 Lille, France.ORCID 0000-0002-2603-962X
Mira Abou DiabUMR Transfrontalière BioEcoAgro N_1158, Institut Charles Viollette, National Research Institute for Agriculture, Food and the Environment, Université Lille, F-59000 Lille, France.
Jihen DhaouefiUMR Transfrontalière BioEcoAgro N_1158, Institut Charles Viollette, National Research Institute for Agriculture, Food and the Environment, Université Lille, F-59000 Lille, France.
Bernard GressierLaboratory of Pharmacology, Pharmacokinetics and Clinical Pharmacy, Faculty of Pharmaceutical and Biological Sciences, University of Lille, 3, rue du Professeur Laguesse, B.P. 83, F-59000 Lille, France.
Bruno EtoLaboratoire TBC, Laboratory of Pharmacology, Pharmacokinetics, and Clinical Pharmacy, Faculty of Pharmaceutical and Biological Sciences, University of Lille, 3, rue du ProfesseurLaguesse, B.P. 83, F-59000 Lille, France.ORCID 0000-0001-9397-2690
Naïma NedjarUMR Transfrontalière BioEcoAgro N_1158, Institut Charles Viollette, National Research Institute for Agriculture, Food and the Environment, Université Lille, F-59000 Lille, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study focuses on the enzymatic hydrolysis of hemoglobin, the main component of cruor that gives blood its red color in mammals. The antibacterial and antioxidant potentials of human hemoglobin hydrolysates were evaluated in comparison to bovine hemoglobin. The results showed strong antimicrobial activity of the peptide hydrolysates against six bacterial strains, independent of the initial substrate concentration level. The hydrolysates also showed strong antioxidant activity, as measured by four different tests. In addition, the antimicrobial and antioxidant activities of the human and bovine hemoglobin hydrolysates showed little or no significant difference, with only the concentration level being the determining factor in their activity. The results of the mass spectrometry study showed the presence of a number of bioactive peptides, the majority of which have characteristics similar to those mentioned in the literature. New bioactive peptides were also identified in human hemoglobin, such as the antibacterial peptides PTTKTYFPHF (α37-46), FPTTKTYFPH (α36-45), TSKYR (α137-141), and STVLTSKYR (α133-141), as well as the antioxidant TSKYR (α137-141). According to these findings, human hemoglobin represents a promising source of bioactive peptides beneficial to the food or pharmaceutical industries.

Indexed as

Anti-Infective AgentsAntioxidantsAnimalsAnti-Bacterial AgentsHemoglobinsHumansHydrolysisMammalsPeptidesAnti-Bacterial AgentsAnti-Infective AgentsAntioxidantsHemoglobinsPeptidesantibacterial activityantioxidant activitybioactive peptidesbovine hemoglobinhuman hemoglobin

Identifiers

PMID37685861
PMCPMC10487712

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.