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ORIGINAL RESEARCH article

Front. Microbiol.

Sec. Food Microbiology

This article is part of the Research TopicProbiotic Potential: Lactic Acid Bacteria in Advancing Functional Foods and Health OutcomesView all 3 articles

Antibacterial potential of a new glucosaminidase from Pediococcus acidilactici ITV26 against Gram negative and Gram-positive pathogens

Provisionally accepted
Karla  G Alvarez-VillagomezKarla G Alvarez-VillagomezDaniel  BallezaDaniel Balleza*Carolina  Peña-MontesCarolina Peña-MontesItzel  C. Fonseca-BarreraItzel C. Fonseca-BarreraPatricia  G. Mendoza-GarcíaPatricia G. Mendoza-García
  • Instituto Tecnológico de Veracruz, Veracruz, Mexico

The final, formatted version of the article will be published soon.

Pediococcus acidilactici is a homofermentative lactic acid bacterium capable of producing pediocins that restrict the proliferation of pathogenic bacteria. However, these bacteria have also been described to produce several peptidoglycan hydrolases (PGH) with great antibacterial potential. These enzymes have been classified as enzybiotics, i.e. proteins capable of degrading cell walls in a highly specific manner to killing pathogens. In this study, we report the compositional, physicochemical, and biochemical characterization of an enzyme with N-acetylglucosaminidase activity produced by P. acidilactici ITV26. This activity is enriched in the membrane fraction of the bacteria and shows a high specificity for Micrococcus lysodeikticus ATCC 4698 cell walls. The protein was purified from this fraction enriched in P. acidilactici membranes, finding a molecular mass close to 110 kDa, a sequence of 935 amino acid residues, a possible transmembrane fragment close to the N-terminal end, and a profile of high intrinsic flexibility with high hydrophilicity, consistent with a possible topology for a This is a provisional file, not the final typeset article peripheral membrane protein. This PGH ITV26 enzyme induces significant autolytic activity in P. acidilactici under acidic conditions and is strongly active against four pathogenic bacteria, including: Staphylococcus aureus ATCC 6538 and ATCC 25923, Clostridium perfrigens ATCC 12916, Klebsiella pneumoniae ATCC 10031 and Pseudomonas aeruginosa ATCC 25619. The ultrastructural effects on each bacterium were studied by scanning electron microscopy (SEM), finding that the effect of this potential enzybiotic destroys the polysaccharide capsule of K. pneumoniae as well as it induces important morphological changes in S. aureus and P. aeruginosa. The absence of hemolytic activity suggests that this enzyme has pharmacological potential against multidrug-resistant bacteria.

Keywords: Peptidoglycan (PG) hydrolases, N-acetylglucosaminidase (NAGase), Autolysis, enzybiotics, Pediococcus acidilactici

Received: 20 Oct 2025; Accepted: 24 Nov 2025.

Copyright: © 2025 Alvarez-Villagomez, Balleza, Peña-Montes, Fonseca-Barrera and Mendoza-García. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

* Correspondence: Daniel Balleza

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