The use of forced protein evolution to investigate and improve stability of family 10 xylanases. The production of Ca2+-independent stable xylanases.
Andrews
Simon R
SR
Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW, UK.
Taylor
Edward J
EJ
Pell
Gavin
G
Vincent
Florence
F
Ducros
Valérie M-A
VM
Davies
Gideon J
GJ
Lakey
Jeremy H
JH
Gilbert
Harry J
HJ
D001665:Binding Sites; D002118:Calcium / Q000378:metabolism / Q000494:pharmacology*; D020633:Cellvibrio / Q000201:enzymology*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003460:Crystallization; D019020:Directed Molecular Evolution; D004220:Disulfides / Q000737:chemistry; D004351:Drug Resistance; D004492:Edetic Acid / Q000494:pharmacology; D043364:Endo-1,4-beta Xylanases; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D006358:Hot Temperature; D006860:Hydrogen Bonding; D016296:Mutagenesis; D016297:Mutagenesis, Site-Directed; D010447:Peptide Hydrolases / Q000494:pharmacology; D016133:Polymerase Chain Reaction; D017510:Protein Folding; D011994:Recombinant Proteins; D013329:Structure-Activity Relationship; D013438:Sulfhydryl Compounds / Q000032:analysis; D013816:Thermodynamics; D014995:Xylosidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D004220:Disulfides; D011994:Recombinant Proteins; D013438:Sulfhydryl Compounds; D004492:Edetic Acid; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases; D010447:Peptide Hydrolases; D002118:Calcium