Engineering the thermotolerance and pH optimum of family 11 xylanases by site-directed mutagenesis. (Q51637027)

8 April 2018

title

Engineering the thermotolerance and pH optimum of family 11 xylanases by site-directed mutagenesis. (English)

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8 April 2018

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Ossi Turunen

1

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8 April 2018

Janne Jänis

series ordinal

2

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8 April 2018

Fred Fenel

series ordinal

3

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8 April 2018

Matti Leisola

series ordinal

4

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8 April 2018

language of work or name

English

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publication date

1 January 2004

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8 April 2018

published in

Methods in Enzymology

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8 April 2018

volume

388

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8 April 2018

page(s)

156-167

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8 April 2018

describes a project that uses

site-directed mutagenesis

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Xylanases: from biology to biotechnology

inferred from title

cites work

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Structural and functional properties of low molecular weight endo-1,4-beta-xylanases

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Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability

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Functional conformational changes of endo-1,4-xylanase II fromTrichoderma reesei: A molecular dynamics study

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Thermostability of endo-1,4-beta-xylanase II from Trichoderma reesei studied by electrospray ionization Fourier-transform ion cyclotron resonance MS, hydrogen/deuterium-exchange reactions and dynamic light scattering

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A combination of weakly stabilizing mutations with a disulfide bridge in the alpha-helix region of Trichoderma reesei endo-1,4-beta-xylanase II increases the thermal stability through synergism

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Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds

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A de novo designed N-terminal disulphide bridge stabilizes the Trichoderma reesei endo-1,4-beta-xylanase II.

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An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: structural basis and molecular study

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Engineering of multiple arginines into the Ser/Thr surface of Trichoderma reesei endo-1,4-beta-xylanase II increases the thermotolerance and shifts the pH optimum towards alkaline pH.

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Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase

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Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase

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Site-directed mutagenesis study of a conserved residue in family 10 glycanases: histidine 86 of xylanase A from Streptomyces lividans

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Characterizing the pH-dependent stability and catalytic mechanism of the family 11 xylanase from the alkalophilic Bacillus agaradhaerens

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SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

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Optimizing the hydrogen-bond network in Poisson-Boltzmann equation-based pK(a) calculations.

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Soluble chromogenic substrates for the assay of endo-1,4-beta-xylanases and endo-1,4-beta-glucanases

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Protein analysis by hydrogen exchange mass spectrometry

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Cloning of the xynB gene from Dictyoglomus thermophilum Rt46B.1 and action of the gene product on kraft pulp

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7 January 2021

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Identifiers

DOI

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8 April 2018

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8 April 2018