about
In the light of directed evolution: pathways of adaptive protein evolutionEngineering hyperthermostability into a GH11 xylanase is mediated by subtle changes to protein structurePredicting changes in protein thermostability brought about by single- or multi-site mutationsA role for A-to-I RNA editing in temperature adaptationImprovement in thermostability of metagenomic GH11 endoxylanase (Mxyl) by site-directed mutagenesis and its applicability in paper pulp bleaching process.Concommitant adaptation of a GH11 xylanase by directed evolution to create an alkali-tolerant/thermophilic enzyme.Thermostable artificial enzyme isolated by in vitro selection.Stabilization of Bacillus circulans xylanase by combinatorial insertional fusion to a thermophilic host protein.From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymesRapid discovery and optimization of therapeutic antibodies against emerging infectious diseases.Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquidsStabilizing biocatalysts.Determination of the modes of action and synergies of xylanases by analysis of xylooligosaccharide profiles over time using fluorescence-assisted carbohydrate electrophoresis.Seven N-terminal residues of a thermophilic xylanase are sufficient to confer hyperthermostability on its mesophilic counterpart.Molecular Determinants for Protein Stabilization by Insertional Fusion to a Thermophilic Host Protein.Laboratory Evolution of Bacillus circulans Xylanase Inserted into Pyrococcus furiosus Maltodextrin-Binding Protein for Increased Xylanase Activity and Thermal Stability Toward Alkaline pH.Improving the thermostability of a methyl parathion hydrolase by adding the ionic bond on protein surface.Systematic optimization of interface interactions increases the thermostability of a multimeric enzyme.Directed evolution of an extremely stable fluorescent protein.Computational design of variants for cephalosporin C acylase from Pseudomonas strain N176 with improved stability and activity.An appraisal of the enzyme stability-activity trade-off.
P2860
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P2860
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
An evolutionary route to xylanase process fitness.
@ast
An evolutionary route to xylanase process fitness.
@en
type
label
An evolutionary route to xylanase process fitness.
@ast
An evolutionary route to xylanase process fitness.
@en
prefLabel
An evolutionary route to xylanase process fitness.
@ast
An evolutionary route to xylanase process fitness.
@en
P2093
P2860
P356
P1433
P1476
An evolutionary route to xylanase process fitness.
@en
P2093
Brian A Steer
Dan E Robertson
Eric J Mathur
Florence Goubet
Geoffery L Tomlinson
Geoffrey P Hazlewood
Gerhard Frey
Jay M Short
John Verruto
P2860
P304
P356
10.1110/PS.03333504
P577
2004-01-10T00:00:00Z