The Multi Domain Caldicellulosiruptor bescii CelA Cellulase Excels at the Hydrolysis of Crystalline Cellulose
Abstract
The crystalline nature of cellulose microfibrils is one of the key factors influencing biomass recalcitrance which is a key technical and economic barrier to overcome to make cellulosic biofuels a commercial reality. To date, all known fungal enzymes tested have great difficulty degrading highly crystalline cellulosic substrates. We have demonstrated that the CelA cellulase from Caldicellulosiruptor bescii degrades highly crystalline cellulose as well as low crystallinity substrates making it the only known cellulase to function well on highly crystalline cellulose. Unlike the secretomes of cellulolytic fungi, which typically comprise multiple, single catalytic domain enzymes for biomass degradation, some bacterial systems employ an alternative strategy that utilizes multi-catalytic domain cellulases. Additionally, CelA is extremely thermostable and highly active at elevated temperatures, unlike commercial fungal cellulases. Furthermore we have determined that the factors negatively affecting digestion of lignocellulosic materials by C. bescii enzyme cocktails containing CelA appear to be significantly different from the performance barriers affecting fungal cellulases. Furthermore, we explore the activity and degradation mechanism of CelA on a variety of pretreated substrates to better understand how the different bulk components of biomass, such as xylan and lignin, impact its performance.
- Authors:
-
[1];
[2];
- National Renewable Energy Lab. (NREL), Golden, CO (United States)
- Novozymes, Inc., Davis, CA (United States)
- Univ. of Georgia, Athens, GA (United States)
- Publication Date:
- Research Org.:
- National Renewable Energy Laboratory (NREL), Golden, CO (United States)
- Sponsoring Org.:
- USDOE Office of Energy Efficiency and Renewable Energy (EERE), Energy Efficiency Office. Building Technologies Office
- OSTI Identifier:
- 1389737
- Report Number(s):
- NREL/JA-2700-68492
Journal ID: ISSN 2045-2322
- Grant/Contract Number:
- AC36-08GO28308
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Scientific Reports
- Additional Journal Information:
- Journal Volume: 7; Journal Issue: 1; Journal ID: ISSN 2045-2322
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 09 BIOMASS FUELS; cellulosic biofuels; biomass; recalcitrance
Citation Formats
Brunecky, Roman, Donohoe, Bryon S., Yarbrough, John M., Mittal, Ashutosh, Scott, Brian R., Ding, Hanshu, Taylor II, Larry E., Russell, Jordan F., Chung, Daehwan, Westpheling, Janet, Teter, Sarah A., Himmel, Michael E., and Bomble, Yannick J. The Multi Domain Caldicellulosiruptor bescii CelA Cellulase Excels at the Hydrolysis of Crystalline Cellulose. United States: N. p., 2017.
Web. doi:10.1038/s41598-017-08985-w.
Brunecky, Roman, Donohoe, Bryon S., Yarbrough, John M., Mittal, Ashutosh, Scott, Brian R., Ding, Hanshu, Taylor II, Larry E., Russell, Jordan F., Chung, Daehwan, Westpheling, Janet, Teter, Sarah A., Himmel, Michael E., & Bomble, Yannick J. The Multi Domain Caldicellulosiruptor bescii CelA Cellulase Excels at the Hydrolysis of Crystalline Cellulose. United States. https://doi.org/10.1038/s41598-017-08985-w
Brunecky, Roman, Donohoe, Bryon S., Yarbrough, John M., Mittal, Ashutosh, Scott, Brian R., Ding, Hanshu, Taylor II, Larry E., Russell, Jordan F., Chung, Daehwan, Westpheling, Janet, Teter, Sarah A., Himmel, Michael E., and Bomble, Yannick J. Tue .
"The Multi Domain Caldicellulosiruptor bescii CelA Cellulase Excels at the Hydrolysis of Crystalline Cellulose". United States. https://doi.org/10.1038/s41598-017-08985-w. https://www.osti.gov/servlets/purl/1389737.
@article{osti_1389737,
title = {The Multi Domain Caldicellulosiruptor bescii CelA Cellulase Excels at the Hydrolysis of Crystalline Cellulose},
author = {Brunecky, Roman and Donohoe, Bryon S. and Yarbrough, John M. and Mittal, Ashutosh and Scott, Brian R. and Ding, Hanshu and Taylor II, Larry E. and Russell, Jordan F. and Chung, Daehwan and Westpheling, Janet and Teter, Sarah A. and Himmel, Michael E. and Bomble, Yannick J.},
abstractNote = {The crystalline nature of cellulose microfibrils is one of the key factors influencing biomass recalcitrance which is a key technical and economic barrier to overcome to make cellulosic biofuels a commercial reality. To date, all known fungal enzymes tested have great difficulty degrading highly crystalline cellulosic substrates. We have demonstrated that the CelA cellulase from Caldicellulosiruptor bescii degrades highly crystalline cellulose as well as low crystallinity substrates making it the only known cellulase to function well on highly crystalline cellulose. Unlike the secretomes of cellulolytic fungi, which typically comprise multiple, single catalytic domain enzymes for biomass degradation, some bacterial systems employ an alternative strategy that utilizes multi-catalytic domain cellulases. Additionally, CelA is extremely thermostable and highly active at elevated temperatures, unlike commercial fungal cellulases. Furthermore we have determined that the factors negatively affecting digestion of lignocellulosic materials by C. bescii enzyme cocktails containing CelA appear to be significantly different from the performance barriers affecting fungal cellulases. Furthermore, we explore the activity and degradation mechanism of CelA on a variety of pretreated substrates to better understand how the different bulk components of biomass, such as xylan and lignin, impact its performance.},
doi = {10.1038/s41598-017-08985-w},
journal = {Scientific Reports},
number = 1,
volume = 7,
place = {United States},
year = {Tue Aug 29 00:00:00 EDT 2017},
month = {Tue Aug 29 00:00:00 EDT 2017}
}
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Deletion of Caldicellulosiruptor besciiCelA reveals its crucial role in the deconstruction of lignocellulosic biomass
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- Biotechnology for Biofuels, Vol. 7, Issue 1
Techno-economic evaluation of integrated first- and second-generation ethanol production from grain and straw
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