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Background <p>Lytic Polysaccharide Monooxygenases (LPMOs) are monocopper oxidative enzymes classified within auxiliary activity (AA) families AA9-AA11 and AA13-AA17 in the CAZy database. LPMOs act synergistically with Glycoside Hydrolases (GHs) to break complex polysaccharides by oxidatively cleaving glycosidic linkages and enhancing substrate accessibility and improving the saccharification efficiency in industrial biomass conversion processes. While extensively studied in fungi and cellulolytic bacteria, LPMOs have remained uncharacterized in enterococcal taxa. The study presents the genomic and functional analysis of AA10-LPMOs from <i>Enterococcus mundtii</i> CRi_37, a strain not previously associated with stubble saccharification.</p> Methods and results <p>This study reports the first functional and genomic characterization of AA10-LPMOs from <i>Enterococcus mundtii</i> CRi_37, a strain not previously linked to stubble biomass deconstruction. Under biotin and cellobiose supplementation, CRi_37 produced 224.04 ± 6.1&#xa0;mg/g reducing sugars from carboxymethyl cellulose and 187.24 ± 5.01&#xa0;mg/g from NaOH-pretreated wheat straw, demonstrating notable saccharification potential. Genome analysis revealed six putative <i>Em</i>AA10 LPMO genes and a diverse CAZyme repertoire comprising 72 GHs, 39 glycosyltransferases, 33 carbohydrate-binding modules, 25 carbohydrate esterases, 16 polysaccharide lyases, and 12 auxiliary activity enzymes. All <i>Em</i>LPMOs exhibited accessory Fibronectin III, E-set, and CBM domains, while <i>Em</i>AA10E uniquely featured Trp<sup>−</sup>⁴ and Ser⁺² substitutions potentially linked to xylanolytic activity.</p> Conclusions <p>The absence of virulence genes underscores CRi_37’s safety for industrial applications. Homology modeling and sequence analysis of <i>Em</i>AA10 LPMOs establish a basis for designing chimeric enzymes with broadened substrate specificity. These findings highlight the metabolic versatility of CRi_37 as a promising resource for sustainable stubble biomass valorization.</p>

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Functional characterization of Lytic Polysaccharide Monooxygenase from Enterococcus mundtii CRi_37 for enhanced stubble saccharification

  • 期刊论文

  • 发表日期：

    2025年9月30日

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  • Sejal Bhairam,
  • Rashi Bamrotwar,
  • Chetana Akhand,
  • Nishant A. Dafale

摘要

Background

Lytic Polysaccharide Monooxygenases (LPMOs) are monocopper oxidative enzymes classified within auxiliary activity (AA) families AA9-AA11 and AA13-AA17 in the CAZy database. LPMOs act synergistically with Glycoside Hydrolases (GHs) to break complex polysaccharides by oxidatively cleaving glycosidic linkages and enhancing substrate accessibility and improving the saccharification efficiency in industrial biomass conversion processes. While extensively studied in fungi and cellulolytic bacteria, LPMOs have remained uncharacterized in enterococcal taxa. The study presents the genomic and functional analysis of AA10-LPMOs from Enterococcus mundtii CRi_37, a strain not previously associated with stubble saccharification.

Methods and results

This study reports the first functional and genomic characterization of AA10-LPMOs from Enterococcus mundtii CRi_37, a strain not previously linked to stubble biomass deconstruction. Under biotin and cellobiose supplementation, CRi_37 produced 224.04 ± 6.1 mg/g reducing sugars from carboxymethyl cellulose and 187.24 ± 5.01 mg/g from NaOH-pretreated wheat straw, demonstrating notable saccharification potential. Genome analysis revealed six putative EmAA10 LPMO genes and a diverse CAZyme repertoire comprising 72 GHs, 39 glycosyltransferases, 33 carbohydrate-binding modules, 25 carbohydrate esterases, 16 polysaccharide lyases, and 12 auxiliary activity enzymes. All EmLPMOs exhibited accessory Fibronectin III, E-set, and CBM domains, while EmAA10E uniquely featured Trp−⁴ and Ser⁺² substitutions potentially linked to xylanolytic activity.

Conclusions

The absence of virulence genes underscores CRi_37’s safety for industrial applications. Homology modeling and sequence analysis of EmAA10 LPMOs establish a basis for designing chimeric enzymes with broadened substrate specificity. These findings highlight the metabolic versatility of CRi_37 as a promising resource for sustainable stubble biomass valorization.