Evidence for substrate binding of a recombinant thermostable xylanase originating from Rhodothermus marinus

Research output: Contribution to journalArticle


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

  • Biochemistry and Molecular Biology


  • Carbohydrate binding domain, Rhodothermus marinus, Thermostable, Xylanase
Original languageEnglish
Pages (from-to)1-7
Number of pages7
JournalFEMS Microbiology Letters
Issue number1
Publication statusPublished - 1998 Nov 1
Publication categoryResearch