Carbohydrate-Binding Module O-mannosylation Alters Binding Selectivity to Cellulose and Lignin

Yaohao Li, Xiaoyang Guan, Patrick Chaffey, Yuan Ruan, Bo Ma, Shiying Shang, Michael Himmel, Gregg Beckham, Hai Long, Zhongping Tan

Research output: Contribution to journalArticlepeer-review

17 Scopus Citations


Improved understanding of the effect of protein glycosylation is expected to provide the foundation for the design of protein glycoengineering strategies. In this study, we examine the impact of O-glycosylation on the binding selectivity of a model Family 1 carbohydrate-binding module (CBM), which has been shown to be one of the primary sub-domains responsible for non-productive lignin binding in multi-modular cellulases. Specifically, we examine the relationship between glycan structure and the binding specificity of the CBM to cellulose and lignin substrates. We find that the glycosylation pattern of the CBM exhibits a strong influence on the binding affinity and the selectivity between both cellulose and lignin. In addition, the large set of binding data collected allows us to examine the relationship between binding affinity and the correlation in motion between pairs of glycosylation sites. Our results suggest that glycoforms displaying highly correlated motion in their glycosylation sites tend to bind cellulose with high affinity and lignin with low affinity. Taken together, this work helps lay the groundwork for future exploitation of glycoengineering as a tool to improve the performance of industrial enzymes.

Original languageAmerican English
Pages (from-to)9262-9271
Number of pages10
JournalChemical Science
Issue number34
StatePublished - 14 Sep 2020

Bibliographical note

Publisher Copyright:
© The Royal Society of Chemistry.

NREL Publication Number

  • NREL/JA-2A00-77968


  • binding energy
  • carbohydrates
  • cellulose
  • glycosylation
  • lignin
  • proteins


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