Evidence map›Paper›PMID 28005227›Full record

ArticlePlant molecular biology2017

In planta production and characterization of a hyperthermostable GH10 xylanase in transgenic sugarcane.

Jae Yoon Kim, Guang Nong, John D Rice, Maria Gallo, James F Preston, Fredy Altpeter

Abstract read
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Article in Plant molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 34% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

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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

6 authors at 2 institutions in 3 countries.

Jae Yoon KimPlant Molecular and Cellular Biology Program, Agronomy Department, Genetics Institute, University of Florida - IFAS, Gainesville, FL, USA.
Guang NongDepartment of Microbiology and Cell Science, University of Florida - IFAS, Gainesville, FL, USA.
John D RiceDepartment of Microbiology and Cell Science, University of Florida - IFAS, Gainesville, FL, USA.
Maria GalloPlant Molecular and Cellular Biology Program, Agronomy Department, Genetics Institute, University of Florida - IFAS, Gainesville, FL, USA.
James F PrestonDepartment of Microbiology and Cell Science, University of Florida - IFAS, Gainesville, FL, USA.
Fredy AltpeterPlant Molecular and Cellular Biology Program, Agronomy Department, Genetics Institute, University of Florida - IFAS, Gainesville, FL, USA. altpeter@ufl.edu.ORCID http://orcid.org/0000-0002-0894-4976
University of Florida · USKorea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sugarcane (Saccharum sp. hybrids) is one of the most efficient and sustainable feedstocks for commercial production of fuel ethanol. Recent efforts focus on the integration of first and second generation bioethanol conversion technologies for sugarcane to increase biofuel yields. This integrated process will utilize both the cell wall bound sugars of the abundant lignocellulosic sugarcane residues in addition to the sucrose from stem internodes. Enzymatic hydrolysis of lignocellulosic biomass into its component sugars requires significant amounts of cell wall degrading enzymes. In planta production of xylanases has the potential to reduce costs associated with enzymatic hydrolysis but has been reported to compromise plant growth and development. To address this problem, we expressed a hyperthermostable GH10 xylanase, xyl10B in transgenic sugarcane which displays optimal catalytic activity at 105 °C and only residual catalytic activity at temperatures below 70 °C. Transgene integration and expression in sugarcane were confirmed by Southern blot, RT-PCR, ELISA and western blot following biolistic co-transfer of minimal expression cassettes of xyl10B and the selectable neomycin phosphotransferase II. Xylanase activity was detected in 17 transgenic lines with a fluorogenic xylanase activity assay. Up to 1.2% of the total soluble protein fraction of vegetative progenies with integration of chloroplast targeted expression represented the recombinant Xyl10B protein. Xyl10B activity was stable in vegetative progenies. Tissues retained 75% of the xylanase activity after drying of leaves at 35 °C and a 2 month storage period. Transgenic sugarcane plants producing Xyl10B did not differ from non-transgenic sugarcane in growth and development under greenhouse conditions. Sugarcane xylan and bagasse were used as substrate for enzymatic hydrolysis with the in planta produced Xyl10B. TLC and HPLC analysis of hydrolysis products confirmed the superior catalytic activity and stability of the in planta produced Xyl10B with xylobiose as a prominent degradation product. These findings will contribute to advancing consolidated processing of lignocellulosic sugarcane biomass.

Indexed as

Hot TemperatureBiocatalysisBlotting, SouthernBlotting, WesternCelluloseDisaccharidesEndo-1,4-beta XylanasesEnzyme-Linked Immunosorbent AssayEnzyme StabilityGene Expression Regulation, EnzymologicPlants, Genetically ModifiedReverse Transcriptase Polymerase Chain ReactionSaccharumSubstrate SpecificityXylansbagasseCelluloseDisaccharidesEndo-1,4-beta XylanasesXylansxylobioseHyperthermostable GH10 endo-1,4-β-xylanase B (Xyl10B)Lignocellulosic bioethanolSaccharum sp. hybridsTransgenic sugarcane

Identifiers

PMID28005227
OpenAlexW2562316529

What OpenQuestion holds

Textmetadata
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Registered trials

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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.