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Fusion of family 2b carbohydrate‐binding module increases the catalytic activity of a xylanase from Thermotoga maritima to soluble xylan
Author(s) -
Kittur Farooqahmed S.,
Mangala Selanere L.,
Rus’d Ahmed Abu,
Kitaoka Motomitsu,
Tsujibo Hiroshi,
Hayashi Kiyoshi
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00803-2
Subject(s) - thermotoga maritima , xylan , xylanase , carbohydrate binding module , chemistry , biochemistry , fusion , carbohydrate , catalysis , food science , polysaccharide , enzyme , glycoside hydrolase , escherichia coli , gene , linguistics , philosophy
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.