The thermostabilizing domain, XynA, of Caldibacillus cellulovorans xylanase is a xylan binding domain
Autor: | A, Sunna, M D, Gibbs, P L, Bergquist |
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Rok vydání: | 2000 |
Předmět: |
Clostridium
endocrine system animal structures Endo-1 4-beta Xylanases Base Sequence Sequence Homology Amino Acid Molecular Sequence Data technology industry and agriculture Temperature macromolecular substances carbohydrates (lipids) Xylosidases Electrophoresis Polyacrylamide Gel Xylans Amino Acid Sequence DNA Primers Protein Binding Research Article |
Zdroj: | The Biochemical journal. |
ISSN: | 0264-6021 |
Popis: | We show that the N-terminal 'thermostabilizing domain' (TSD) of the xylanase, XynA, from the thermophilic bacterium Caldibacillus cellulovorans also acts as a xylan binding domain. Affinity electrophoresis experiments show that this TSD selectively binds soluble xylan and binds weakly to hydroxyethylcellulose. Based on this, and previously reported evidence, we propose that xylanase-associated TSDs are xylan binding domains. |
Databáze: | OpenAIRE |
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