Evidence map›Paper›PMID 33407766›Full record

ArticleBiotechnology for biofuels2021

Chimeric cellobiohydrolase I expression, activity, and biochemical properties in three oleaginous yeast.

Markus Alahuhta, Qi Xu, Eric P Knoshaug, Wei Wang, Hui Wei, Antonella Amore, John O Baker, Todd Vander Wall, Michael E Himmel, Min Zhang

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 41% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Markus AlahuhtaBiosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA. markus.alahuhta@nrel.gov.ORCID http://orcid.org/0000-0001-9375-778X
Qi XuBiosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA.
Eric P KnoshaugBiosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA.
Wei WangBiosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA.
Hui WeiBiosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA.
Antonella AmoreBiosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA.
John O BakerBiosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA.
Todd Vander WallBiosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA.
Michael E HimmelBiosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA.
Min ZhangBiosciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA. min.zhang@nrel.gov.
National Laboratory of the Rockies · US

Funding

Office of Energy Efficiency and Renewable Energy DE-AC36-08GO28308
6 · The paper itself

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.

Indexed as

CBH ICel7ACellobiohydrolaseConsolidated bioprocessingMetabolic engineering: chimeric proteinOleaginous yeast

Identifiers

PMID33407766
PMCPMC7789491
OpenAlexW3120726701

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.