Glycosylation Is Vital for Industrial Performance of Hyperactive Cellulases

Yannick Bomble, Daehwan Chung, Brandon Knott, Neal Hengge, John Yarbrough, Roman Brunecky, Todd VanderWall, Michael Crowley, Michael Himmel, Jordan Russell, Jenna Young, Nitin Supekar, Christine Szymanski, Lance Wells, Parastoo Azadi, Janet Westpheling, Nicholas Sarai, Deanne Sammond

Research output: Contribution to journalArticlepeer-review

19 Scopus Citations

Abstract

In the terrestrial biosphere, biomass deconstruction is conducted by microbes employing a variety of complementary strategies, many of which remain to be discovered. Moreover, the biofuels industry seeks more efficient (and less costly) cellulase formulations upon which to launch the nascent sustainable bioenergy economy. The glycan decoration of fungal cellulases has been shown to protect these enzymes from protease action and to enhance binding to cellulose. We show here that thermal tolerant bacterial cellulases are glycosylated as well, although the types and extents of decoration differ from their Eukaryotic counterparts. Our major findings are that glycosylation of CelA is uniform across its three linker peptides and composed of mainly galactose disaccharides (which is unique) and that this glycosylation dramatically impacts the hydrolysis of insoluble substrates, proteolytic and thermal stability, and substrate binding and changes the dynamics of the enzyme. This study suggests that the glycosylation of CelA is crucial for its exceptionally high cellulolytic activity on biomass and provides the robustness needed for this enzyme to function in harsh environments including industrial settings.

Original languageAmerican English
Pages (from-to)4792-4800
Number of pages9
JournalACS Sustainable Chemistry and Engineering
Volume7
Issue number5
DOIs
StatePublished - 4 Mar 2019

Bibliographical note

Publisher Copyright:
© Copyright 2019 American Chemical Society.

NREL Publication Number

  • NREL/JA-2700-73100

Keywords

  • Biofuels
  • Caldicellulosiruptor bescii
  • CAZymes
  • Cellulolytic anaerobes
  • Enzyme stability
  • Galactose
  • Glycosylation

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