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<p>Cellulose is the most abundant biomass on Earth, and its enzymatic hydrolysis by cellulases, such as Endoglucanases, has great industrial potential. This study structurally characterized, through homology modeling and molecular dynamics (MD), an Endoglucanase from Moniliophthora perniciosa (GH45, sequence 10760), focusing on a catalytic site mutation. The model, based on the Glycosyl Hydrolase from Thielavia terrestris (PDB: 5GLY), showed a satisfactory QMEAN value (− 1.09) in SWISSMODEL and 92.96% of residues in favorable regions by Ramachandran plot. GH45 model and the crystallographic template were subjected to 100&#xa0;ns MD simulations (GROMOS54a7 force field) complexed with cellotetraose (CTT) and cellotriose (CTR). RMSD and RMSF analyses indicate stable trajectories for both complexes. In the catalytic site, where tryptophan was replaced by cysteine, RMSF values were slightly lower in GH45 than the template. Interaction maps confirmed that the mutation doesn't affect catalysis, and GH45-10,670 retains its potential as a biocatalytic material for bioethanol production.</p> Graphical abstract <p></p>

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Investigation of the structure and dynamic behavior of endoglucanase (GH45) from Moniliphthora perniciosa for second generation bioethanol (2G) production

  • 期刊论文

  • 发表日期：

    2026年2月25日

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  • Alison Borges Vitor,
  • Luiz Henrique Machado Oliveira,
  • Raquel Guimarães Benevides,
  • Luciano Sergio Hocevar,
  • Carine Tondo Alves

摘要

Cellulose is the most abundant biomass on Earth, and its enzymatic hydrolysis by cellulases, such as Endoglucanases, has great industrial potential. This study structurally characterized, through homology modeling and molecular dynamics (MD), an Endoglucanase from Moniliophthora perniciosa (GH45, sequence 10760), focusing on a catalytic site mutation. The model, based on the Glycosyl Hydrolase from Thielavia terrestris (PDB: 5GLY), showed a satisfactory QMEAN value (− 1.09) in SWISSMODEL and 92.96% of residues in favorable regions by Ramachandran plot. GH45 model and the crystallographic template were subjected to 100 ns MD simulations (GROMOS54a7 force field) complexed with cellotetraose (CTT) and cellotriose (CTR). RMSD and RMSF analyses indicate stable trajectories for both complexes. In the catalytic site, where tryptophan was replaced by cysteine, RMSF values were slightly lower in GH45 than the template. Interaction maps confirmed that the mutation doesn't affect catalysis, and GH45-10,670 retains its potential as a biocatalytic material for bioethanol production.

Graphical abstract