Engineering enhanced cellobiohydrolase activity

Larry E. Taylor, Brandon C. Knott, John O. Baker, P. Markus Alahuhta, Sarah E. Hobdey, Jeffrey G. Linger, Vladimir V. Lunin, Antonella Amore, Venkataramanan Subramanian, Kara Podkaminer, Qi Xu, Todd A. VanderWall, Logan A. Schuster, Yogesh B. Chaudhari, William S. Adney, Michael F. Crowley, Michael E. Himmel, Stephen R. Decker () and Gregg T. Beckham ()
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Larry E. Taylor: National Renewable Energy Laboratory
Brandon C. Knott: National Renewable Energy Laboratory
John O. Baker: National Renewable Energy Laboratory
P. Markus Alahuhta: National Renewable Energy Laboratory
Sarah E. Hobdey: National Renewable Energy Laboratory
Jeffrey G. Linger: National Renewable Energy Laboratory
Vladimir V. Lunin: National Renewable Energy Laboratory
Antonella Amore: National Renewable Energy Laboratory
Venkataramanan Subramanian: National Renewable Energy Laboratory
Kara Podkaminer: National Renewable Energy Laboratory
Qi Xu: National Renewable Energy Laboratory
Todd A. VanderWall: National Renewable Energy Laboratory
Logan A. Schuster: National Renewable Energy Laboratory
Yogesh B. Chaudhari: National Renewable Energy Laboratory
William S. Adney: National Renewable Energy Laboratory
Michael F. Crowley: National Renewable Energy Laboratory
Michael E. Himmel: National Renewable Energy Laboratory
Stephen R. Decker: National Renewable Energy Laboratory
Gregg T. Beckham: National Renewable Energy Laboratory

Nature Communications, 2018, vol. 9, issue 1, 1-10

Abstract: Abstract Glycoside Hydrolase Family 7 cellobiohydrolases (GH7 CBHs) catalyze cellulose depolymerization in cellulolytic eukaryotes, making them key discovery and engineering targets. However, there remains a lack of robust structure–activity relationships for these industrially important cellulases. Here, we compare CBHs from Trichoderma reesei (TrCel7A) and Penicillium funiculosum (PfCel7A), which exhibit a multi-modular architecture consisting of catalytic domain (CD), carbohydrate-binding module, and linker. We show that PfCel7A exhibits 60% greater performance on biomass than TrCel7A. To understand the contribution of each domain to this improvement, we measure enzymatic activity for a library of CBH chimeras with swapped subdomains, demonstrating that the enhancement is mainly caused by PfCel7A CD. We solve the crystal structure of PfCel7A CD and use this information to create a second library of TrCel7A CD mutants, identifying a TrCel7A double mutant with near-equivalent activity to wild-type PfCel7A. Overall, these results reveal CBH regions that enable targeted activity improvements.

Date: 2018
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DOI: 10.1038/s41467-018-03501-8

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