Autohydrolysis of plant xylans by apoplastic expression of thermophilic bacterial endo-xylanases

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Autohydrolysis of plant xylans by apoplastic expression of thermophilic bacterial endo-xylanases. / Borkhardt, Bernhard; Harholt, Jesper; Ulvskov, Peter Bjarne; Ahring, Birgitte Kiær; Jørgensen, Bodil; Brinch-Pedersen, Henrik.

In: Plant Biotechnology Journal, Vol. 8, No. 3, 2010, p. 363-374.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Borkhardt, B, Harholt, J, Ulvskov, PB, Ahring, BK, Jørgensen, B & Brinch-Pedersen, H 2010, 'Autohydrolysis of plant xylans by apoplastic expression of thermophilic bacterial endo-xylanases', Plant Biotechnology Journal, vol. 8, no. 3, pp. 363-374. https://doi.org/10.1111/j.1467-7652.2010.00506.x

APA

Borkhardt, B., Harholt, J., Ulvskov, P. B., Ahring, B. K., Jørgensen, B., & Brinch-Pedersen, H. (2010). Autohydrolysis of plant xylans by apoplastic expression of thermophilic bacterial endo-xylanases. Plant Biotechnology Journal, 8(3), 363-374. https://doi.org/10.1111/j.1467-7652.2010.00506.x

Vancouver

Borkhardt B, Harholt J, Ulvskov PB, Ahring BK, Jørgensen B, Brinch-Pedersen H. Autohydrolysis of plant xylans by apoplastic expression of thermophilic bacterial endo-xylanases. Plant Biotechnology Journal. 2010;8(3):363-374. https://doi.org/10.1111/j.1467-7652.2010.00506.x

Author

Borkhardt, Bernhard ; Harholt, Jesper ; Ulvskov, Peter Bjarne ; Ahring, Birgitte Kiær ; Jørgensen, Bodil ; Brinch-Pedersen, Henrik. / Autohydrolysis of plant xylans by apoplastic expression of thermophilic bacterial endo-xylanases. In: Plant Biotechnology Journal. 2010 ; Vol. 8, No. 3. pp. 363-374.

Bibtex

@article{2fc184906e1e11df928f000ea68e967b,
title = "Autohydrolysis of plant xylans by apoplastic expression of thermophilic bacterial endo-xylanases",
abstract = "The genes encoding the two endo-xylanases XynA and XynB from the thermophilic bacterium Dictyoglomus thermophilum were codon optimized for expression in plants. Both xylanases were designed to be constitutively expressed under the control of the CaMV 35S promoter and targeted to the apoplast. Transient expression in tobacco and stable expression in transgenic Arabidopsis showed that both enzymes were expressed in an active form with temperature optima at 85 °C. Transgenic Arabidopsis accumulating heterologous endo-xylanases appeared phenotypically normal and were fully fertile. The highest xylanase activity in Arabidopsis was found in dry stems indicating that the enzymes were not degraded during stem senescence. High levels of enzyme activity were maintained in cell-free extracts from dry transgenic stems during incubation at 85 °C for 24 h. Analysis of cell wall polysaccharides after heat treatment of wildtype and transgenic extracts from dry stems showed a decrease in the molecular weight of xylans from transgenic stems.",
author = "Bernhard Borkhardt and Jesper Harholt and Ulvskov, {Peter Bjarne} and Ahring, {Birgitte Ki{\ae}r} and Bodil J{\o}rgensen and Henrik Brinch-Pedersen",
year = "2010",
doi = "10.1111/j.1467-7652.2010.00506.x",
language = "English",
volume = "8",
pages = "363--374",
journal = "Plant Biotechnology Journal",
issn = "1467-7644",
publisher = "Wiley-Blackwell",
number = "3",

}

RIS

TY - JOUR

T1 - Autohydrolysis of plant xylans by apoplastic expression of thermophilic bacterial endo-xylanases

AU - Borkhardt, Bernhard

AU - Harholt, Jesper

AU - Ulvskov, Peter Bjarne

AU - Ahring, Birgitte Kiær

AU - Jørgensen, Bodil

AU - Brinch-Pedersen, Henrik

PY - 2010

Y1 - 2010

N2 - The genes encoding the two endo-xylanases XynA and XynB from the thermophilic bacterium Dictyoglomus thermophilum were codon optimized for expression in plants. Both xylanases were designed to be constitutively expressed under the control of the CaMV 35S promoter and targeted to the apoplast. Transient expression in tobacco and stable expression in transgenic Arabidopsis showed that both enzymes were expressed in an active form with temperature optima at 85 °C. Transgenic Arabidopsis accumulating heterologous endo-xylanases appeared phenotypically normal and were fully fertile. The highest xylanase activity in Arabidopsis was found in dry stems indicating that the enzymes were not degraded during stem senescence. High levels of enzyme activity were maintained in cell-free extracts from dry transgenic stems during incubation at 85 °C for 24 h. Analysis of cell wall polysaccharides after heat treatment of wildtype and transgenic extracts from dry stems showed a decrease in the molecular weight of xylans from transgenic stems.

AB - The genes encoding the two endo-xylanases XynA and XynB from the thermophilic bacterium Dictyoglomus thermophilum were codon optimized for expression in plants. Both xylanases were designed to be constitutively expressed under the control of the CaMV 35S promoter and targeted to the apoplast. Transient expression in tobacco and stable expression in transgenic Arabidopsis showed that both enzymes were expressed in an active form with temperature optima at 85 °C. Transgenic Arabidopsis accumulating heterologous endo-xylanases appeared phenotypically normal and were fully fertile. The highest xylanase activity in Arabidopsis was found in dry stems indicating that the enzymes were not degraded during stem senescence. High levels of enzyme activity were maintained in cell-free extracts from dry transgenic stems during incubation at 85 °C for 24 h. Analysis of cell wall polysaccharides after heat treatment of wildtype and transgenic extracts from dry stems showed a decrease in the molecular weight of xylans from transgenic stems.

U2 - 10.1111/j.1467-7652.2010.00506.x

DO - 10.1111/j.1467-7652.2010.00506.x

M3 - Journal article

C2 - 20384855

VL - 8

SP - 363

EP - 374

JO - Plant Biotechnology Journal

JF - Plant Biotechnology Journal

SN - 1467-7644

IS - 3

ER -

ID: 20119508