Evidence for substrate binding of a recombinant thermostable xylanase originating from Rhodothermus marinus
(1998) In FEMS Microbiology Letters 168(1). p.1-7- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/61b1a91e-54f5-44d0-8bd6-40096aae0579
- author
- Nordberg Karlsson, Eva LU ; Bartonek-Roxå, Eva LU and Holst, Olle LU
- organization
- publishing date
- 1998-11-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Carbohydrate binding domain, Rhodothermus marinus, Thermostable, Xylanase
- in
- FEMS Microbiology Letters
- volume
- 168
- issue
- 1
- pages
- 7 pages
- publisher
- Oxford University Press
- external identifiers
-
- scopus:0032211894
- pmid:9812357
- ISSN
- 0378-1097
- DOI
- 10.1016/S0378-1097(98)00404-2
- language
- English
- LU publication?
- yes
- id
- 61b1a91e-54f5-44d0-8bd6-40096aae0579
- date added to LUP
- 2018-11-14 21:15:09
- date last changed
- 2024-04-15 16:37:30
@article{61b1a91e-54f5-44d0-8bd6-40096aae0579, abstract = {{<p>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.</p>}}, author = {{Nordberg Karlsson, Eva and Bartonek-Roxå, Eva and Holst, Olle}}, issn = {{0378-1097}}, keywords = {{Carbohydrate binding domain; Rhodothermus marinus; Thermostable; Xylanase}}, language = {{eng}}, month = {{11}}, number = {{1}}, pages = {{1--7}}, publisher = {{Oxford University Press}}, series = {{FEMS Microbiology Letters}}, title = {{Evidence for substrate binding of a recombinant thermostable xylanase originating from Rhodothermus marinus}}, url = {{http://dx.doi.org/10.1016/S0378-1097(98)00404-2}}, doi = {{10.1016/S0378-1097(98)00404-2}}, volume = {{168}}, year = {{1998}}, }