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

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:
Report Number(s):
NREL/JA-2700-71961
Journal ID: ISSN 0001-1541
Grant/Contract Number:
AC36-08GO28308; P200A160061; P200A100004-12
Type:
Accepted Manuscript
Journal Name:
AIChE Journal
Additional Journal Information:
Journal Name: AIChE Journal; Journal ID: ISSN 0001-1541
Publisher:
American Institute of Chemical Engineers
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)
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; Caldicellulosiruptor; lignocellulose; glycoside hydrolase; cellulase
OSTI Identifier:
1475518
Alternate Identifier(s):
OSTI ID: 1464583

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., 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.. 2018. "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 = ,
volume = ,
place = {United States},
year = {2018},
month = {7}
}

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