Evidence map›Paper›PMID 26528471›Full record

ArticleFrontiers in bioengineering and biotechnology2015

Development of a High Throughput Platform for Screening Glycoside Hydrolases Based on Oxime-NIMS.

Kai Deng, Joel M Guenther, Jian Gao, Benjamin P Bowen, Huu Tran, Vimalier Reyes-Ortiz, Xiaoliang Cheng, Noppadon Sathitsuksanoh, Richard Heins, Taichi E Takasuka and 10 more

Abstract read
In one paragraph

Article in Frontiers in bioengineering and biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
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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

20 authors.

Kai DengUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Sandia National Laboratories , Livermore, CA , USA.
Joel M GuentherUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Sandia National Laboratories , Livermore, CA , USA.
Jian GaoLawrence Berkeley National Laboratory , Berkeley, CA , USA.
Benjamin P BowenLawrence Berkeley National Laboratory , Berkeley, CA , USA.
Huu TranUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Sandia National Laboratories , Livermore, CA , USA.
Vimalier Reyes-OrtizUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Lawrence Berkeley National Laboratory , Berkeley, CA , USA.
Xiaoliang ChengUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Lawrence Berkeley National Laboratory , Berkeley, CA , USA.
Noppadon SathitsuksanohUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Lawrence Berkeley National Laboratory , Berkeley, CA , USA.
Richard HeinsUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Sandia National Laboratories , Livermore, CA , USA.
Taichi E TakasukaUS Department of Energy Great Lakes Bioenergy Research Center, University of Wisconsin , Madison, WI , USA.
Lai F BergemanUS Department of Energy Great Lakes Bioenergy Research Center, University of Wisconsin , Madison, WI , USA.
Henrik Geertz-HansenUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA.
Samuel DeutschLawrence Berkeley National Laboratory , Berkeley, CA , USA ; Joint Genome Institute , Walnut Creek, CA , USA.
Dominique LoquéUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Lawrence Berkeley National Laboratory , Berkeley, CA , USA.
Kenneth L SaleUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Sandia National Laboratories , Livermore, CA , USA.
Blake A SimmonsUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Sandia National Laboratories , Livermore, CA , USA.
Paul D AdamsUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Lawrence Berkeley National Laboratory , Berkeley, CA , USA ; Department of Bioengineering, University of California Berkeley , Berkeley, CA , USA.
Anup K SinghUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Sandia National Laboratories , Livermore, CA , USA.
Brian G FoxUS Department of Energy Great Lakes Bioenergy Research Center, University of Wisconsin , Madison, WI , USA ; Department of Biochemistry, University of Wisconsin , Madison, WI , USA.
Trent R NorthenUS Department of Energy Joint BioEnergy Institute , Emeryville, CA , USA ; Lawrence Berkeley National Laboratory , Berkeley, CA , USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cost-effective hydrolysis of biomass into sugars for biofuel production requires high-performance low-cost glycoside hydrolase (GH) cocktails that are active under demanding process conditions. Improving the performance of GH cocktails depends on knowledge of many critical parameters, including individual enzyme stabilities, optimal reaction conditions, kinetics, and specificity of reaction. With this information, rate- and/or yield-limiting reactions can be potentially improved through substitution, synergistic complementation, or protein engineering. Given the wide range of substrates and methods used for GH characterization, it is difficult to compare results across a myriad of approaches to identify high performance and synergistic combinations of enzymes. Here, we describe a platform for systematic screening of GH activities using automatic biomass handling, bioconjugate chemistry, robotic liquid handling, and nanostructure-initiator mass spectrometry (NIMS). Twelve well-characterized substrates spanning the types of glycosidic linkages found in plant cell walls are included in the experimental workflow. To test the application of this platform and substrate panel, we studied the reactivity of three engineered cellulases and their synergy of combination across a range of reaction conditions and enzyme concentrations. We anticipate that large-scale screening using the standardized platform and substrates will generate critical datasets to enable direct comparison of enzyme activities for cocktail design.

Indexed as

cellulaseenzyme assayshigh throughput screeningNIMSoxime bioconjugation

Identifiers

PMID26528471
PMCPMC4603251

What OpenQuestion holds

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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.