z-logo
open-access-imgOpen Access
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here