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Updated: Aug 13, 2025

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
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Exploring how lignin structure influences the interaction between carbohydrate-binding module and lignin using AFM.

Hui Chen1, Bo Jiang1, Chunyang Zou2

  • 1Jiangsu Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, College of Light Industry and Food Engineering, Nanjing Forestry University, Nanjing 210037, China; Joint International Research Lab of Lignocellulosic Functional Materials, International Innovation Center for Forest Chemicals and Materials, Nanjing Forestry University, Nanjing 210037, China.

International Journal of Biological Macromolecules
|January 22, 2023
PubMed
Summary

Sulfonated lignin significantly reduces cellulase adsorption, enhancing enzymatic hydrolysis of lignocellulose. This competitive adsorption mechanism explains improved biomass conversion efficiency.

Keywords:
Carbohydrate-binding module (CBM)LigninSingle-molecule interaction

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Area of Science:

  • Biomass Conversion and Bioenergy
  • Biochemistry and Molecular Biology
  • Materials Science

Background:

  • Nonproductive adsorption of cellulase onto lignin hinders efficient enzymatic hydrolysis of lignocellulose.
  • Understanding lignin's structural impact on cellulase interaction is crucial for optimizing biofuel production.

Purpose of the Study:

  • To quantitatively investigate the effect of lignin structure on its interaction with cellulase.
  • To elucidate the mechanism by which sulfonated lignin enhances lignocellulose enzymatic hydrolysis.

Main Methods:

  • Utilized atomic force microscopy (AFM) with a carbohydrate-binding module (CBM) functionalized tip.
  • Employed single-molecule dynamic force spectroscopy (DFS) to measure CBM-lignin adhesion forces.
  • Investigated the effect of sulfonated lignin (SL) on CBM-lignin interactions.

Main Results:

  • Sulfonated lignin (SL) exhibited the highest adhesion force to CBM (4.74 nN), followed by Masson pine MWL (2.85 nN), poplar MWL (1.03 nN), and herbaceous MWLs (0.27–0.61 nN).
  • Addition of SL drastically reduced CBM-MWL interactions to 0.054–0.083 nN.
  • Demonstrated that SL significantly reduces nonproductive adsorption of lignin onto cellulase.

Conclusions:

  • Lignin structure critically influences its interaction with cellulase, impacting enzymatic hydrolysis efficiency.
  • Sulfonated lignin promotes lignocellulose hydrolysis primarily by competitively adsorbing to cellulase, thereby reducing nonproductive binding to substrate lignin.
  • Proposed a 'competitive adsorption' mechanism to explain SL's effectiveness in enhancing enzymatic hydrolysis of lignin-containing substrates.