
Effect of Glycosylation and Additional Domains on the Thermostability of a Family 10 Xylanase Produced by Thermopolyspora flexuosa
Author(s) -
Sasikala Anbarasan,
Janne Jänis,
Marja Paloheimo,
Mikko Laitaoja,
Minna Vuolanto,
Johanna Karimäki,
Pirjo Vainiotalo,
Matti Leisola,
Ossi Turunen
Publication year - 2010
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.00357-09
Subject(s) - thermostability , xylanase , glycosylation , chemistry , biochemistry , carbohydrate binding module , carbohydrate , enzyme , food science , glycoside hydrolase
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.