Novel Multidomain, Multifunctional Glycoside Hydrolases from Highly Lignocellulolytic Caldicellulosiruptor Species

Vladimir Lunin, Petri Alahuhta, Michael Himmel, Yannick Bomble, Jonathan Conway, James Crosby, Andrew Hren, Robert Southerland, Laura Lee, Michael Adams, Robert Kelly

Research output: Contribution to journalArticlepeer-review

21 Scopus Citations


Biological hydrolysis of microcrystalline cellulose is an uncommon feature in the microbial world, especially among bacteria and archaea growing optimally above 70°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.

Original languageAmerican English
Pages (from-to)4218-4228
Number of pages11
JournalAIChE Journal
Issue number12
StatePublished - 2018

Bibliographical note

Publisher Copyright:
© 2018 American Institute of Chemical Engineers

NREL Publication Number

  • NREL/JA-2700-71961


  • Caldicellulosiruptor
  • cellulase
  • glycoside hydrolase
  • lignocellulose


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