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Title: 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:
 [1];  [2];  [1];  [1];  [3];  [1];  [1];  [3];  [3];  [1]; ORCiD logo [1]; ORCiD logo [1];  [3];  [3];  [3];  [3];  [1]; ORCiD logo [1]
  1. National Renewable Energy Lab. (NREL), Golden, CO (United States)
  2. National Renewable Energy Lab. (NREL), Golden, CO (United States); California Inst. of Technology (CalTech), Pasadena, CA (United States)
  3. 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) (SC-22)
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. 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., and Bomble, Yannick J. Fri . "Glycosylation Is Vital for Industrial Performance of Hyperactive Cellulases". United States. doi: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}
}

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Works referencing / citing this record:

Engineering Geobacillus thermoglucosidasius for direct utilisation of holocellulose from wheat straw
journal, August 2019