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

FEBS Letters

Hayashi, Kiyoshi²  Kittur, Farooqahmed S.²  Kitaoka, Motomitsu²  Mangala, Selanere L.²  Rus’d, Ahmed Abu²  Tsujibo, Hiroshi¹ 

[1] Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1041, Japan;Enzyme Laboratory, National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan

关键词: Xylanase;    Thermostable;    Carbohydrate-binding module;    Chimeric enzyme;   

DOI  :  10.1016/S0014-5793(03)00803-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown