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Title: Carbohydrate-binding module O-mannosylation alters binding selectivity to cellulose and lignin

Journal Article · · Chemical Science
DOI: https://doi.org/10.1039/d0sc01812k · OSTI ID:1648588

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.

Research Organization:
National Renewable Energy Laboratory (NREL), Golden, CO (United States)
Sponsoring Organization:
USDOE Office of Energy Efficiency and Renewable Energy (EERE), Transportation Office. Bioenergy Technologies Office; National Key Research and Development Program of China; National Major Scientific and Technological Special Project of China; National Natural Science Foundation of China (NSFC); USDOE
Grant/Contract Number:
AC36-08GO28308; 2018YFE0111400; 2018ZX09711001-013; 91853120
OSTI ID:
1648588
Alternate ID(s):
OSTI ID: 1669625
Report Number(s):
NREL/JA-2A00-77968; MainId:31877; UUID:2225c987-5e02-4390-87ab-e1b0a5996afc; MainAdminID:18608
Journal Information:
Chemical Science, Vol. 11, Issue 34; ISSN 2041-6520
Publisher:
Royal Society of ChemistryCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 9 works
Citation information provided by
Web of Science

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Figures / Tables (5)