Chimeric Cellobiohydrolase I Expression, Activity, and Biochemical Properties in Three Oleaginous Yeast

Petri Alahuhta, Qi Xu, Eric Knoshaug, Wei Wang, Hui Wei, Antonella Amore, John Baker, Todd VanderWall, Michael Himmel, Min Zhang

Research output: Contribution to journalArticlepeer-review

3 Scopus Citations

Abstract

Consolidated bioprocessing using oleaginous yeast is a promising modality for the economic conversion of plant biomass to fuels and chemicals. However, yeast are not known to produce effective biomass degrading enzymes naturally and this trait is essential for efficient consolidated bioprocessing. We expressed a chimeric cellobiohydrolase I gene in three different oleaginous, industrially relevant yeast: Yarrowia lipolytica, Lipomyces starkeyi, and Saccharomyces cerevisiae to study the biochemical and catalytic properties and biomass deconstruction potential of these recombinant enzymes. Our results showed differences in glycosylation, surface charge, thermal and proteolytic stability, and efficacy of biomass digestion. L. starkeyi was shown to be an inferior active cellulase producer compared to both the Y. lipolytica and S. cerevisiae enzymes, whereas the cellulase expressed in S. cerevisiae displayed the lowest activity against dilute-acid-pretreated corn stover. Comparatively, the chimeric cellobiohydrolase I enzyme expressed in Y. lipolytica was found to have a lower extent of glycosylation, better protease stability, and higher activity against dilute-acid-pretreated corn stover.

Original languageAmerican English
Article number6
Number of pages11
JournalBiotechnology for Biofuels
Volume14
Issue number1
DOIs
StatePublished - 2021

Bibliographical note

Publisher Copyright:
© 2021, The Author(s).

NREL Publication Number

  • NREL/JA-2700-77142

Keywords

  • CBH I
  • Cel7A
  • Cellobiohydrolase
  • Consolidated bioprocessing
  • Metabolic engineering: chimeric protein
  • Oleaginous yeast

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