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

Eva Nordberg Karlsson, Eva Bartonek-Roxå, Olle Holst

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)1-7
Number of pages7
JournalFEMS Microbiology Letters
Volume168
Issue number1
DOIs
Publication statusPublished - 1998 Nov 1

Subject classification (UKÄ)

  • Biochemistry and Molecular Biology

Free keywords

  • Carbohydrate binding domain
  • Rhodothermus marinus
  • Thermostable
  • Xylanase

Fingerprint

Dive into the research topics of 'Evidence for substrate binding of a recombinant thermostable xylanase originating from Rhodothermus marinus'. Together they form a unique fingerprint.

Cite this