AEM Accepts, published online ahead of print on 23 October 2009

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Appl. Environ. Microbiol. doi:10.1128/AEM.00357-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The Effect of glycosylation and additional domains on the thermostability of a family 10 xylanase of Thermopolyspora flexuosa

Sasikala Anbarasan, Janne Jänis, Marja Paloheimo, Mikko Laitaoja, Minna Vuolanto, Johanna Karimäki, Pirjo Vainiotalo, Matti Leisola, and Ossi Turunen^*

Department of Biotechnology and Chemical Technology, Helsinki University of Technology, P.O.Box 6100, 02015 TKK, Finland; Department of Chemistry, University of Joensuu, P.O. Box 111, 80101 Joensuu, Finland; Roal Oy, P.O. Box 57, 05201 Rajamäki, Finland

^* To whom correspondence should be addressed. Email: Ossi.Turunen{at}hut.fi.

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 thermostability of XYN10A. In contrast, glycosylation at Asn-26, located in an exposed loop, decreased thermostability. The presence of a substrate increased stability mainly at low pH.