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Glycosylation Is Vital for Industrial Performance of Hyperactive Cellulases

Chung, Daehwan and Sarai, Nicholas S. and Knott, Brandon C. and Hengge, Neal and Russell, Jordan F. and Yarbrough, John M. and Brunecky, Roman and Young, Jenna and Supekar, Nitin and Vander Wall, Todd and Sammond, Deanne W. and Crowley, Michael F. and Szymanski, Christine M. and Wells, Lance and Azadi, Parastoo and Westpheling, Janet and Himmel, Michael E. and Bomble, Yannick J. (2019) Glycosylation Is Vital for Industrial Performance of Hyperactive Cellulases. ACS Sustainable Chemistry & Engineering, 7 (5). pp. 4792-4800. ISSN 2168-0485. doi:10.1021/acssuschemeng.8b05049.

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In the terrestrial biosphere, biomass deconstruction is conducted by microbes employing a variety of complementary strategies, many of which remain to be discovered. Moreover, the biofuels industry seeks more efficient (and less costly) cellulase formulations upon which to launch the nascent sustainable bioenergy economy. The glycan decoration of fungal cellulases has been shown to protect these enzymes from protease action and to enhance binding to cellulose. We show here that thermal tolerant bacterial cellulases are glycosylated as well, although the types and extents of decoration differ from their Eukaryotic counterparts. Our major findings are that glycosylation of CelA is uniform across its three linker peptides and composed of mainly galactose disaccharides (which is unique) and that this glycosylation dramatically impacts the hydrolysis of insoluble substrates, proteolytic and thermal stability, and substrate binding and changes the dynamics of the enzyme. This study suggests that the glycosylation of CelA is crucial for its exceptionally high cellulolytic activity on biomass and provides the robustness needed for this enzyme to function in harsh environments including industrial settings.

Item Type:Article
Related URLs:
URLURL TypeDescription Information
Sarai, Nicholas S.0000-0002-4655-0038
Sammond, Deanne W.0000-0002-5911-1309
Crowley, Michael F.0000-0001-5163-9398
Bomble, Yannick J.0000-0001-7624-8000
Additional Information:© 2019 American Chemical Society. Received: October 1, 2018; Revised: December 4, 2018; Published: February 1, 2019. Funding provided by the BioEnergy Science Center (BESC) and the Center for Bioenergy Innovation (CBI), from the U.S. Department of Energy Bioenergy Research Centers supported by the Office of Biological and Environmental Research in the DOE Office of Science. This research was also supported in part by the National Institutes of Health grants 1S10OD018530 and P41GM10349010 and the Chemical Sciences, Geosciences and Biosciences Division, Office of Basic Energy Sciences, U.S. Department of Energy grant (DE-FG02-93ER20097) at the Complex Carbohydrate Research Center. This work was authored in part by Alliance for Sustainable Energy, LLC, the Manager and Operator of the National Renewable Energy Laboratory for the U.S. Department of Energy (DOE) under Contract No. DE-AC36-08GO28308. The views expressed in the article do not necessarily represent the views of the DOE or the U.S. Government. The U.S. Government retains and the publisher, by accepting the article for publication, acknowledges that the U.S. Government retains a nonexclusive, paid-up, irrevocable, worldwide license to publish or reproduce the published form of this work, or allow others to do so, for U.S. Government purposes. The authors declare no competing financial interest.
Funding AgencyGrant Number
Department of Energy (DOE)DE-FG02-93ER20097
Department of Energy (DOE)DE-AC36-08GO28308
Issue or Number:5
Record Number:CaltechAUTHORS:20190321-113934405
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Official Citation:Glycosylation Is Vital for Industrial Performance of Hyperactive Cellulases. Daehwan Chung, Nicholas S. Sarai, Brandon C. Knott, Neal Hengge, Jordan F. Russell, John M. Yarbrough, Roman Brunecky, Jenna Young, Nitin Supekar, Todd Vander Wall, Deanne W. Sammond, Michael F. Crowley, Christine M. Szymanski, Lance Wells, Parastoo Azadi, Janet Westpheling, Michael E. Himmel, and Yannick J. Bomble. ACS Sustainable Chemistry & Engineering 2019 7 (5), 4792-4800. DOI: 10.1021/acssuschemeng.8b05049
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:94019
Deposited By: Tony Diaz
Deposited On:21 Mar 2019 21:57
Last Modified:16 Nov 2021 17:02

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