Open AccessEvidence for substrate binding of a recombinant thermostable xylanase originating from Rhodothermus marinus
Author(s) -
Nordberg Karlsson Eva,
BartonekRoxå Eva,
Holst Olle
Publication year - 1998
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1998.tb13247.x
Subject(s) - xylanase , thermophile , recombinant dna , xylan , biochemistry , cellulose , bacteria , binding domain , chemistry , binding site , biology , enzyme , genetics , gene
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.