Heterologous co-expression of two β-glucanases and a cellobiose phosphorylase resulted in a significant increase in the cellulolytic activity of the Caldicellulosiruptor bescii exoproteome

Sun Ki Kim, Daehwan Chung, Michael E. Himmel, Yannick J. Bomble, Janet Westpheling

Research output: Contribution to journalArticlepeer-review

10 Scopus Citations

Abstract

The ability to deconstruct plant biomass without conventional pretreatment has made members of the genus Caldicellulosiruptor the target of investigation for the consolidated processing of plant lignocellulosic biomass to biofuels and bioproducts. To investigate the synergy of enzymes involved and to further improve the ability of C. bescii to degrade cellulose, we introduced CAZymes that act synergistically with the C. bescii exoproteome in vivo and in vitro. We recently demonstrated that the Acidothermus cellulolyticus E1 endo-1,4-β-D-glucanase (GH5) with a family 2 carbohydrate-binding module (CBM) increased the activity of C. bescii exoproteome on biomass, presumably acting in concert with CelA. The β-glucanase, GuxA, from A. cellulolyticus is a multi-domain enzyme with strong processive exoglucanase activity, and the cellobiose phosphorylase from Thermotoga maritima catalyzes cellulose degradation acting synergistically with cellobiohydrolases and endoglucanases. We identified new chromosomal insertion sites to co-express these enzymes and the resulting strain showed a significant increase in the enzymatic activity of the exoproteome.

Original languageAmerican English
Pages (from-to)687-695
Number of pages9
JournalJournal of Industrial Microbiology and Biotechnology
Volume46
Issue number5
DOIs
StatePublished - 2019

Bibliographical note

Publisher Copyright:
© 2019, Society for Industrial Microbiology and Biotechnology.

NREL Publication Number

  • NREL/JA-2700-73412

Keywords

  • Biomass deconstruction
  • Caldicellulosiruptor
  • Cellobiose phosphorylase
  • Consolidated bioprocessing
  • Gene integration
  • Glucanase

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