title: Assembling a novel bifunctional cellulase-xylanase from Thermotoga maritima by end-to-end fusion.
abstract: 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.
authors.affiliation: Division of Applied Life Science, Gyeongsang National University, Chinju, 660-701, Republic of Korea.
authors.forename: Su Young
authors.initials: SY
authors.lastname: Hong
authors.forename: Jin Suk
authors.initials: JS
authors.lastname: Lee
authors.forename: Kye Man
authors.initials: KM
authors.lastname: Cho
authors.forename: Renukaradhya K
authors.initials: RK
authors.lastname: Math
authors.forename: Yong Hee
authors.initials: YH
authors.lastname: Kim
authors.forename: Sun Joo
authors.initials: SJ
authors.lastname: Hong
authors.forename: Yong Un
authors.initials: YU
authors.lastname: Cho
authors.forename: Hoon
authors.initials: H
authors.lastname: Kim
authors.forename: Han Dae
authors.initials: HD
authors.lastname: Yun
mesh_terms: 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
chemical_list: D004798:Enzymes; D011993:Recombinant Fusion Proteins; D002482:Cellulose; D004247:DNA; D014995:Xylosidases; D002480:Cellulase