Evidence map›Paper›PMID 41291579›Full record

ArticleBMC biotechnology2025

Protease sensitivity and stress adaptation of bioactive peptide-producing lactic acid bacteria: functional implications for food biopreservation.

Oluwabukola Atinuke Popoola, Abimbola Ayodeji Orukotan, Olubunmi Olaitan Agarry

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Article in BMC biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Oluwabukola Atinuke PopoolaGenetics, Genomics and Bioinformatics Department, National Biotechnology Research and Development Agency (NBRDA), Abuja, Nigeria. atinuke.solina@gmail.com.ORCID 0009-0006-2202-6967
Abimbola Ayodeji OrukotanCollege of Basic Sciences, Lagos State University of Science and Technology, Ikorodu, Lagos, Nigeria.ORCID 0000-0002-0833-5652
Olubunmi Olaitan AgarryDepartment of Microbiology, University of Abuja, Abuja, Nigeria.ORCID 0000-0002-5354-1180

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe search for safe, natural food preservatives has turned attention to antimicrobial peptide (AMP)-producing lactic acid bacteria (LAB). These AMPs, which are bioactive peptides of proteinaceous nature, inhibit a broad spectrum of foodborne pathogens. Their proteinaceous composition ensures safety and digestibility; however, their effectiveness depends on the physiological resilience of the producing LAB under food-relevant stresses and the susceptibility of the AMPs to proteolytic degradation.

resultsThe 13 AMP-producing LAB strains tolerated a wide pH range (4.5–8.5), multiple temperatures (20–45 °C), and moderate to high salt concentrations (5.5–10% NaCl), demonstrating robustness under diverse food processing and storage conditions. Even after exposure to these physiological stresses, the strains retained antimicrobial activity, producing zones of inhibition ranging from 5 mm under extreme stress conditions to 20 mm under optimum growth conditions against Staphylococcus aureus ATCC 25923 and Escherichia coli ATCC 25922. The antimicrobial peptides were completely inactivated by protease treatments with pepsin, trypsin, proteinase K, and papain, confirming their proteinaceous nature while highlighting protease susceptibility. Six of the 13 LAB strains had been previously 16S rRNA-sequenced (GenBank accession numbers PV983358–PV983363), including one strain showing 93.54% sequence identity to the closest known species; suggesting potential novelty.

conclusionsAMP-producing LAB from Nigerian non-dairy fermentations exhibit broad physiological adaptability and produce proteinaceous antimicrobial peptides with notable inhibitory activity against foodborne pathogens, even under stress conditions. Although complete protease susceptibility limits in vivo stability, their safety, traceable identification, and environmental robustness underscore their promise as natural, clean-label food preservatives, supporting the development of safe, minimally processed food strategies.

Indexed as

Antimicrobial PeptidesFood PreservationLactobacillalesPeptide HydrolasesAdaptation, PhysiologicalEscherichia coliFood MicrobiologyHydrogen-Ion ConcentrationStaphylococcus aureusStress, PhysiologicalAntimicrobial PeptidesPeptide HydrolasesBioactive peptidesFood biopreservationLactic acid bacteria (LAB)Protease sensitivityStress adaptation

Identifiers

PMID41291579
PMCPMC12752275

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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 OpenQuestion graph.