Fusion of family 2b carbohydrate-binding module increases the catalytic activity of a xylanase from Thermotoga maritima to soluble xylan

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. I...

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Veröffentlicht in:FEBS letters 2003-08, Vol.549 (1), p.147-151
Hauptverfasser: Kittur, Farooqahmed S., Mangala, Selanere L., Rus’d, Ahmed Abu, Kitaoka, Motomitsu, Tsujibo, Hiroshi, Hayashi, Kiyoshi
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Sprache:eng
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Zusammenfassung: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°C. XynB-CBM2b bound to insoluble birchwood and oatspelt xylan. Whereas its hydrolytic activities toward insoluble xylan and p-nitrophenyl-β-xylopyranoside were similar to those of XynB, its activity toward soluble xylan was moderately higher than that of XynB.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(03)00803-2