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. 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.
Kittur
Farooqahmed S
FS
Enzyme Laboratory, National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan.
Mangala
Selanere L
SL
Rus'd
Ahmed Abu
AA
Kitaoka
Motomitsu
M
Tsujibo
Hiroshi
H
Hayashi
Kiyoshi
K
D001426:Bacterial Proteins / Q000235:genetics*; D002352:Carrier Proteins / Q000235:genetics*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D011485:Protein Binding; D011956:Receptors, Cell Surface; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology*; D013696:Temperature; D043325:Xylan Endo-1,3-beta-Xylosidase / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D002352:Carrier Proteins; D011956:Receptors, Cell Surface; D011993:Recombinant Fusion Proteins; C055213:saccharide-binding proteins; D043325:Xylan Endo-1,3-beta-Xylosidase