ArticleProtein science : a publication of the Protein Society2026
The characterization of a new stabilized lactonase from the endophytic fungi Aspergillus pseudonomiae with anti-bacterial and anti-fungal properties.
Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- The characterization of a new stabilized lactonase from the endophytic fungi Aspergillus pseudonomiae with anti-bacterial and anti-fungal properties.Protein science : a publication of the Protein Society · 2026Article
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5 authors.
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Abstract
Microorganisms use diverse small-molecule signals to coordinate behavior, supporting interspecies and interkingdom communication. These chemical dialogs shape fundamental biological processes and define interactions from cooperation to antagonism. Quorum-quenching (QQ) enzymes, which degrade or modify quorum sensing (QS) molecules such as N-acyl-homoserine lactones (AHLs), may play a pivotal role in shaping these networks. While bacterial QQ lactonases are well-characterized, fungal lactonases remain undercharacterized, including their potential to target both bacterial QS molecules and fungal secondary metabolites. Using phylogenetic and structural analysis, we identified putative lactonases from the metallo-β-lactamase-like lactonase family in fungi and biochemically validated the activity of one of them, from Aspergillus pseudonomiae. Structural alignment between bacterial lactonases and the AlphaFold-predicted structure of the fungal homolog further supports that the fungal protein is indeed a lactonase. We then applied Protein Repair One-Stop Shop algorithm for stability engineering to design a variant with improved expression in Escherichia coli and thermal stability. Purified enzyme demonstrated broad substrate specificity, effectively degrading various bacterial AHLs, with k
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