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

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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.

Detaljer

Författare
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biokemi och molekylärbiologi

Nyckelord

Originalspråkengelska
Sidor (från-till)1-7
Antal sidor7
TidskriftFEMS Microbiology Letters
Volym168
Utgåva nummer1
StatusPublished - 1998 nov 1
PublikationskategoriForskning
Peer review utfördJa