Effect of glycosylation and additional domains on the thermostability of a family 10 xylanase produced by Thermopolyspora flexuosa.
The effects of different structural features on the thermostability of Thermopolyspora flexuosa xylanase XYN10A were investigated. A C-terminal carbohydrate binding module had only a slight effect, whereas a polyhistidine tag increased the thermostability of XYN10A xylanase. In contrast, glycosylation at Asn26, located in an exposed loop, decreased the thermostability of the xylanase. The presence of a substrate increased stability mainly at low pH.
Department of Biotechnology and Chemical Technology, Aalto University, P.O. Box 6100, 02015 TKK, Espoo, Finland.
Sasikala
S
Anbarasan
Janne
J
Jänis
Marja
M
Paloheimo
Mikko
M
Laitaoja
Minna
M
Vuolanto
Johanna
J
Karimäki
Pirjo
P
Vainiotalo
Matti
M
Leisola
Ossi
O
Turunen
D000192:Actinomycetales / Q000201:enzymology*; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004795:Enzyme Stability; D006031:Glycosylation; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D017434:Protein Structure, Tertiary / Q000235:genetics
D043364:Endo-1,4-beta Xylanases