Glycosylation Is Vital for Industrial Performance of Hyperactive Cellulases
Abstract
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.
- Authors:
-
- National Renewable Energy Lab. (NREL), Golden, CO (United States)
- National Renewable Energy Lab. (NREL), Golden, CO (United States); California Inst. of Technology (CalTech), Pasadena, CA (United States)
- Univ. of Georgia, Athens, GA (United States)
- Publication Date:
- Research Org.:
- National Renewable Energy Lab. (NREL), Golden, CO (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1497985
- Report Number(s):
- NREL/JA-2700-73100
Journal ID: ISSN 2168-0485
- Grant/Contract Number:
- AC36-08GO28308
- Resource Type:
- Accepted Manuscript
- Journal Name:
- ACS Sustainable Chemistry & Engineering
- Additional Journal Information:
- Journal Volume: 7; Journal Issue: 5; Journal ID: ISSN 2168-0485
- Publisher:
- American Chemical Society (ACS)
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 09 BIOMASS FUELS; biofuels; Caldicellulosiruptor bescii; CAZymes; cellulolytic anaerobes; enzyme stability; galactose; glycosylation
Citation Formats
Chung, Daehwan, Sarai, Nicholas S., Knott, Brandon C., Hengge, Neal, Russell, Jordan F., Yarbrough, John M., Brunecky, Roman, Young, Jenna, Supekar, Nitin, Vander Wall, Todd, Sammond, Deanne W., Crowley, Michael F., Szymanski, Christine M., Wells, Lance, Azadi, Parastoo, Westpheling, Janet, Himmel, Michael E., and Bomble, Yannick J. Glycosylation Is Vital for Industrial Performance of Hyperactive Cellulases. United States: N. p., 2019.
Web. doi:10.1021/acssuschemeng.8b05049.
Chung, Daehwan, Sarai, Nicholas S., Knott, Brandon C., Hengge, Neal, Russell, Jordan F., Yarbrough, John M., Brunecky, Roman, Young, Jenna, Supekar, Nitin, Vander Wall, Todd, Sammond, Deanne W., Crowley, Michael F., Szymanski, Christine M., Wells, Lance, Azadi, Parastoo, Westpheling, Janet, Himmel, Michael E., & Bomble, Yannick J. Glycosylation Is Vital for Industrial Performance of Hyperactive Cellulases. United States. https://doi.org/10.1021/acssuschemeng.8b05049
Chung, Daehwan, Sarai, Nicholas S., Knott, Brandon C., Hengge, Neal, Russell, Jordan F., Yarbrough, John M., Brunecky, Roman, Young, Jenna, Supekar, Nitin, Vander Wall, Todd, Sammond, Deanne W., Crowley, Michael F., Szymanski, Christine M., Wells, Lance, Azadi, Parastoo, Westpheling, Janet, Himmel, Michael E., and Bomble, Yannick J. Fri .
"Glycosylation Is Vital for Industrial Performance of Hyperactive Cellulases". United States. https://doi.org/10.1021/acssuschemeng.8b05049. https://www.osti.gov/servlets/purl/1497985.
@article{osti_1497985,
title = {Glycosylation Is Vital for Industrial Performance of Hyperactive Cellulases},
author = {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.},
abstractNote = {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.},
doi = {10.1021/acssuschemeng.8b05049},
journal = {ACS Sustainable Chemistry & Engineering},
number = 5,
volume = 7,
place = {United States},
year = {2019},
month = {2}
}
Web of Science
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