Assembling a novel bifunctional cellulase-xylanase from Thermotoga maritima by end-to-end fusion.
An artificial, bifunctional, thermostable cellulase-xylanase enzyme from Thermotoga maritima by gene fusion. The fusion protein exhibited both cellulase and xylanase activity when xynA was fused downstream of cel5C but no activities were shown when xynA was fused upstream of cel5C. The enzyme was optimally active at pH 5.0 and 80 degrees C over 30 min. E. coli expressed the fusion enzyme, with an apparent molecular mass of approximately 152 kDa by carboxymethyl cellulose- and xylan-SDS-PAGE.
Hong
Su Young
SY
Division of Applied Life Science, Gyeongsang National University, Chinju, 660-701, Republic of Korea.
Lee
Jin Suk
JS
Cho
Kye Man
KM
Math
Renukaradhya K
RK
Kim
Yong Hee
YH
Hong
Sun Joo
SJ
Cho
Yong Un
YU
Kim
Hoon
H
Yun
Han Dae
HD
D001709:Biotechnology / Q000379:methods*; D002480:Cellulase / Q000737:chemistry*; D002482:Cellulose / Q000737:chemistry; D004247:DNA / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D004798:Enzymes / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D013696:Temperature; D020124:Thermotoga maritima / Q000378:metabolism*; D014995:Xylosidases / Q000737:chemistry* / Q000378:metabolism
D004798:Enzymes; D011993:Recombinant Fusion Proteins; D002482:Cellulose; D004247:DNA; D014995:Xylosidases; D002480:Cellulase