Fusion of family 2b carbohydrate-binding module increases the catalytic activity of a xylanase from Thermotoga maritima to soluble xylan
| Autor: | Selanere L. Mangala, Hiroshi Tsujibo, Kiyoshi Hayashi, Motomitsu Kitaoka, Farooqahmed S. Kittur, Ahmed Abu Rus’d |
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| Jazyk: | angličtina |
| Předmět: |
animal structures
Recombinant Fusion Proteins Biophysics Receptors Cell Surface Plasma protein binding Biochemistry Streptomyces Hydrolysis Chimeric enzyme Bacterial Proteins Structural Biology Genetics Molecular Biology Carbohydrate-binding module Thermostable biology Chemistry Xylanase Temperature Cell Biology Hydrogen-Ion Concentration biology.organism_classification Xylan Xylan Endo-1 3-beta-Xylosidase Thermotoga maritima Carrier Proteins Streptomyces thermoviolaceus Protein Binding |
| Zdroj: | FEBS Letters. (1-3):147-151 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/S0014-5793(03)00803-2 |
| Popis: | A family 2b carbohydrate-binding module from Streptomyces thermoviolaceus STX-II was fused at the carboxyl-terminus of XynB, a thermostable and single domain family 10 xylanase from Thermotoga maritima, to create a chimeric xylanase. The chimeric enzyme (XynB-CBM2b) was purified and characterized. It displayed a pH-activity profile similar to that of XynB and was stable up to 90 degrees C. XynB-CBM2b bound to insoluble birchwood and oatspelt xylan. Whereas its hydrolytic activities toward insoluble xylan and p-nitrophenyl-beta-xylopyranoside were similar to those of XynB, its activity toward soluble xylan was moderately higher than that of XynB. |
| Databáze: | OpenAIRE |
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