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Table · dataset · 2026

Proteomics-Guided Discovery of Candidate Enzymes for Degradation of a Rare Pyruvylated Glycosaminogalactan by a Newly Isolated Luteolibacter Strain

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Bacterial exopolysaccharides (EPS) display extensive structural diversity arising from variation in monosaccharide composition, glycosidic linkages, and non-carbohydrate modifications.

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However, the enzymes responsible for degrading many EPS structures remain unknown, reflecting the limited coverage of current carbohydrate-active enzyme (CAZyme) families. Here, we investigated the microbial degradation of EPS<sub><i>Lp</i></sub>, a high-molecular-mass glycosaminogalactan from Lactiplantibacillus pentosus KW1 containing the uncommon GalNAcβ1 → 2(4,6-<i>O</i>-<i>R</i>-pyruvyl)Gal motif.

Enrichment cultivation with EPS<sub><i>Lp</i></sub> as the main carbon source led to the isolation of <i>Luteolibacter</i> sp. VK1, a novel strain capable of utilizing this biopolymer. Size-exclusion chromatography and MALDI-TOF mass spectrometry showed that VK1 depolymerizes EPS<sub><i>Lp</i></sub> into defined oligosaccharides, consistent with endo-acting cleavage followed by further processing.

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By combining genomics, AlphaFold-based structural annotation and comparative proteomics, we identified candidate CAZymes potentially involved in EPS<sub><i>Lp</i></sub> catabolism. Notably, a secreted GH123 protein and a distantly related GH123-like protein were strongly associated with EPS<sub><i>Lp</i></sub>-dependent growth, suggesting that this enzyme family, or related structural homologues, may contribute to extracellular EPS<sub><i>Lp</i></sub> depolymerization.

Together, these findings support a candidate pathway for degradation of a structurally complex, pyruvylated bacterial glycan and highlight potentially novel EPS-active enzymes whose proposed roles, predicted through bioinformatic analyses, await experimental validation.

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Mass spectrometry 75%
Provenance · 5 source records, 19 field assertions
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