Carbohydrate-Binding Modules Enhance H2O2 Tolerance by Promoting Lytic Polysaccharide Monooxygenase Active Site H2O2 Consumption | [1st International Conference on "Recent Advances in Green Biotechnology and Climate Resilience", September 15-16, 2025 • 2025]

Author(s):

1. Wa Gao: Dalian Engineering Research Center for Carbohydrate Agricultural Preparations, Dalian Technology Innovation Center for Green Agriculture, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences,Dalian,China

2. Tang Li: Dalian Engineering Research Center for Carbohydrate Agricultural Preparations, Dalian Technology Innovation Center for Green Agriculture, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences,Dalian,China

3. Haichuan Zhou: Dalian Engineering Research Center for Carbohydrate Agricultural Preparations, Dalian Technology Innovation Center for Green Agriculture, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences,Dalian,China

4. Jiu Ju: Dalian Engineering Research Center for Carbohydrate Agricultural Preparations, Dalian Technology Innovation Center for Green Agriculture, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences,Dalian,China;

5. Heng Yin: Dalian Engineering Research Center for Carbohydrate Agricultural Preparations, Dalian Technology Innovation Center for Green Agriculture, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences,Dalian,China; University of Chinese Academy of Sciences, Beijing, China

Abstract:

Lytic polysaccharide mono oxygenases (LPMOs) ox datively depolymerize recalcitrant polysaccharides, which is important for biomass conversion. The catalytic domains of many LPMOs are linked to carbohydrate-binding modules(CBMs) through flexible linkers, but the function of these CBMs in LPMO catalysis is not well understood. In this study, we utilized MtLPMO9L andMtLPMO9G derived from Myceliophthora thermophile to investigate the impact of CBMs on LPMO activity, with particular emphasis on their influence onH2O2 tolerance. Using truncated forms of MtLPMO9G generated by removing the CBM, we found reduced substrate binding affinity and enzymatic activity. Conversely, when the CBM was fused to the C terminus of the single-domainMtLPMO9L to create MtLPMO9L-CBM, we observed a substantial improvement in substrate binding affinity, enzymatic activity, and notably,H2O2 tolerance. Furthermore, molecular dynamics simulations confirmed that the CBM fusion enhances the proximity of the active site to the substrate, thereby promoting multifocal cleavage and impacting the exposure of the cooperative site to H2O2. Importantly, the fusion of CBM resulted in more efficient consumption of H2O2 by LPMO, leading to improved enzymatic activity and reduced auto-oxidative damage of the copper active center.

Page(s): 27-287

DOI: DOI not available

Published: Journal: 1st International Conference on "Recent Advances in Green Biotechnology and Climate Resilience", September 15-16, 2025, Volume: 1, Issue: 1, Year: 2025

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