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Title: Novel multidomain, multifunctional glycoside hydrolases from highly lignocellulolytic Caldicellulosiruptor species

Abstract

Biological hydrolysis of microcrystalline cellulose is an uncommon feature in the microbial world, especially among bacteria and archaea growing optimally above 70 degrees C (the so-called extreme thermophiles). In fact, among this group only certain species in the genus Caldicellulosiruptor are capable of rapid and extensive cellulose degradation. Four novel multidomain glycoside hydrolases (GHs) from Caldicellulosiruptor morganii and Caldicellulosiruptor danielii were produced recombinantly in Caldicellulosiruptor bescii and characterized. These GHs are structurally organized with two or three catalytic domains flanking carbohydrate binding modules from Family 3. Collectively, these enzymes represent GH families 5, 9, 10, 12, 44, 48, and 74, and hydrolyze crystalline cellulose, glucan, xylan, and mannan, the primary carbohydrates in plant biomass. Degradation of microcrystalline cellulose by cocktails of GHs from three Caldicellulosiruptor species demonstrated that synergistic interactions enable mixtures of multiple enzymes to outperform single enzymes, suggesting a community mode of action for lignocellulose utilization in thermal environments.

Authors:
 [1];  [1];  [1];  [1];  [1];  [2];  [2];  [2];  [2];  [3]; ORCiD logo [1]
  1. North Carolina State Univ., Raleigh, NC (United States)
  2. National Renewable Energy Lab. (NREL), Golden, CO (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), Biological and Environmental Research (BER) (SC-23)
OSTI Identifier:
1475518
Alternate Identifier(s):
OSTI ID: 1464583
Report Number(s):
NREL/JA-2700-71961
Journal ID: ISSN 0001-1541
Grant/Contract Number:  
AC36-08GO28308; P200A160061; P200A100004-12; GM008776‐11
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
AIChE Journal
Additional Journal Information:
Journal Volume: 64; Journal Issue: 12; Journal ID: ISSN 0001-1541
Publisher:
American Institute of Chemical Engineers
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; Caldicellulosiruptor; lignocellulose; glycoside hydrolase; cellulase

Citation Formats

Conway, Jonathan M., Crosby, James R., Hren, Andrew P., Southerland, Robert T., Lee, Laura L., Lunin, Vladimir V., Alahuhta, Petri, Himmel, Michael E., Bomble, Yannick J., Adams, Michael W. W., and Kelly, Robert M. Novel multidomain, multifunctional glycoside hydrolases from highly lignocellulolytic Caldicellulosiruptor species. United States: N. p., 2018. Web. doi:10.1002/aic.16354.
Conway, Jonathan M., Crosby, James R., Hren, Andrew P., Southerland, Robert T., Lee, Laura L., Lunin, Vladimir V., Alahuhta, Petri, Himmel, Michael E., Bomble, Yannick J., Adams, Michael W. W., & Kelly, Robert M. Novel multidomain, multifunctional glycoside hydrolases from highly lignocellulolytic Caldicellulosiruptor species. United States. doi:10.1002/aic.16354.
Conway, Jonathan M., Crosby, James R., Hren, Andrew P., Southerland, Robert T., Lee, Laura L., Lunin, Vladimir V., Alahuhta, Petri, Himmel, Michael E., Bomble, Yannick J., Adams, Michael W. W., and Kelly, Robert M. Wed . "Novel multidomain, multifunctional glycoside hydrolases from highly lignocellulolytic Caldicellulosiruptor species". United States. doi:10.1002/aic.16354.
@article{osti_1475518,
title = {Novel multidomain, multifunctional glycoside hydrolases from highly lignocellulolytic Caldicellulosiruptor species},
author = {Conway, Jonathan M. and Crosby, James R. and Hren, Andrew P. and Southerland, Robert T. and Lee, Laura L. and Lunin, Vladimir V. and Alahuhta, Petri and Himmel, Michael E. and Bomble, Yannick J. and Adams, Michael W. W. and Kelly, Robert M.},
abstractNote = {Biological hydrolysis of microcrystalline cellulose is an uncommon feature in the microbial world, especially among bacteria and archaea growing optimally above 70 degrees C (the so-called extreme thermophiles). In fact, among this group only certain species in the genus Caldicellulosiruptor are capable of rapid and extensive cellulose degradation. Four novel multidomain glycoside hydrolases (GHs) from Caldicellulosiruptor morganii and Caldicellulosiruptor danielii were produced recombinantly in Caldicellulosiruptor bescii and characterized. These GHs are structurally organized with two or three catalytic domains flanking carbohydrate binding modules from Family 3. Collectively, these enzymes represent GH families 5, 9, 10, 12, 44, 48, and 74, and hydrolyze crystalline cellulose, glucan, xylan, and mannan, the primary carbohydrates in plant biomass. Degradation of microcrystalline cellulose by cocktails of GHs from three Caldicellulosiruptor species demonstrated that synergistic interactions enable mixtures of multiple enzymes to outperform single enzymes, suggesting a community mode of action for lignocellulose utilization in thermal environments.},
doi = {10.1002/aic.16354},
journal = {AIChE Journal},
number = 12,
volume = 64,
place = {United States},
year = {Wed Jul 11 00:00:00 EDT 2018},
month = {Wed Jul 11 00:00:00 EDT 2018}
}

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Works referenced in this record:

Phylogenetic, Microbiological, and Glycoside Hydrolase Diversities within the Extremely Thermophilic, Plant Biomass-Degrading Genus Caldicellulosiruptor
journal, October 2010

  • Blumer-Schuette, S. E.; Lewis, D. L.; Kelly, R. M.
  • Applied and Environmental Microbiology, Vol. 76, Issue 24, p. 8084-8092
  • DOI: 10.1128/AEM.01400-10

Direct conversion of plant biomass to ethanol by engineered Caldicellulosiruptor bescii
journal, June 2014

  • Chung, D.; Cha, M.; Guss, A. M.
  • Proceedings of the National Academy of Sciences, Vol. 111, Issue 24, p. 8931-8936
  • DOI: 10.1073/pnas.1402210111

Protein production by auto-induction in high-density shaking cultures
journal, May 2005


Revealing Nature's Cellulase Diversity The Digestion Mechanism of Caldicellulosiruptor bescii CelA
journal, December 2013


Multidomain and Multifunctional Glycosyl Hydrolases from the Extreme Thermophile Caldicellulosiruptor Isolate Tok7B.1
journal, May 2000

  • Gibbs, Moreland D.; Reeves, Rosalind A.; Farrington, G. King
  • Current Microbiology, Vol. 40, Issue 5, p. 333-340
  • DOI: 10.1007/s002849910066