Evidence for substrate binding of a recombinant thermostable xylanase originating from Rhodothermus marinus
Research output: Contribution to journal › Article
The xyn1 encoded 5 domain xylanase from the thermophilic bacterium Rhodothermus marinus binds specifically to xylan, β-glucan and amorphous but not crystalline cellulose. Our results show that the binding is mediated by the full length xylanase, but not by the catalytic domain only. Based on similarities concerning both predicted secondary structure and binding specificity found with one cellulose binding domain of CenC from Cellulomonas fimi, we suggest that the binding is mediated by the two N-terminally repeated domains. Copyright (C) 1998 Federation of European Microbiological Societies.
|Research areas and keywords||
Subject classification (UKÄ) – MANDATORY
|Number of pages||7|
|Journal||FEMS Microbiology Letters|
|Publication status||Published - 1998 Nov 1|