Construction of the bifunctional enzyme cellulase-β-glucosidase from the hyperthermophilic bacterium Thermotoga maritima

by: Su-Young Hong, Jin-Suk Lee, Kye-Man Cho, Renukaradhya Math, Yong-Hee Kim, Sun-Joo Hong, Yong-Un Cho, Soo-Jeong Cho, Hoon Kim, Han-Dae Yun

Biotechnology Letters, Vol. 29, No. 6. (21 June 2007), pp. 931-936.

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摘要

Abstract An artificial bifunctional enzyme, cellulase-β-glucosidase, was prepared by gene fusion from the hyperthermophilic bacterium Thermotoga maritima MSB8. The fusion protein exhibited both cellulase (Cel5C) and β-glucosidase (BglB) activity when the bglB gene was fused to downstream of cel5C, but not when cel5C was fused to downstream of bglB. The specific activity of the bifunctional enzyme was 70% lower than that of cellulase or β-glucosidase. The fusion enzyme was purified, and the MW was estimated as 114 kDa. The fusion enzyme displayed optimum cellulase activity at pH 8.0 and 70C over 30 min, and optimal β-glucosidase activity at pH 7.0 and 80C over 30 min.

@article{citeulike:1296789, abstract = {Abstract\ \ An artificial bifunctional enzyme, cellulase-β-glucosidase, was prepared by gene fusion from the hyperthermophilic bacterium Thermotoga maritima MSB8. The fusion protein exhibited both cellulase (Cel5C) and β-glucosidase (BglB) activity when the bglB gene was fused to downstream of cel5C, but not when cel5C was fused to downstream of bglB. The specific activity of the bifunctional enzyme was 70\% lower than that of cellulase or β-glucosidase. The fusion enzyme was purified, and the MW was\ estimated as 114\ kDa. The fusion enzyme displayed optimum cellulase activity at pH 8.0 and 70C over 30\ min, and optimal β-glucosidase activity at pH 7.0 and 80C over 30\ min.}, author = {Hong, Su-Young and Lee, Jin-Suk and Cho, Kye-Man and Math, Renukaradhya and Kim, Yong-Hee and Hong, Sun-Joo and Cho, Yong-Un and Cho, Soo-Jeong and Kim, Hoon and Yun, Han-Dae }, citeulike-article-id = {1296789}, doi = {http://dx.doi.org/10.1007/s10529-007-9334-5}, journal = {Biotechnology Letters}, keywords = {gene\_fusion, multifunctional\_enzyme}, month = {June}, number = {6}, pages = {931--936}, posted-at = {2007-05-15 10:29:55}, priority = {2}, title = {Construction of the bifunctional enzyme cellulase-β-glucosidase from the hyperthermophilic bacterium Thermotoga maritima}, url = {http://dx.doi.org/10.1007/s10529-007-9334-5}, volume = {29}, year = {2007} }

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TY - JOUR ID - citeulike:1296789 L3 - citeulike-article-id:1296789 TI - Construction of the bifunctional enzyme cellulase-β-glucosidase from the hyperthermophilic bacterium Thermotoga maritima JF - Biotechnology Letters VL - 29 IS - 6 SP - 931 EP - 936 N2 - Abstract  An artificial bifunctional enzyme, cellulase-β-glucosidase, was prepared by gene fusion from the hyperthermophilic bacterium Thermotoga maritima MSB8. The fusion protein exhibited both cellulase (Cel5C) and β-glucosidase (BglB) activity when the bglB gene was fused to downstream of cel5C, but not when cel5C was fused to downstream of bglB. The specific activity of the bifunctional enzyme was 70% lower than that of cellulase or β-glucosidase. The fusion enzyme was purified, and the MW was estimated as 114 kDa. The fusion enzyme displayed optimum cellulase activity at pH 8.0 and 70C over 30 min, and optimal β-glucosidase activity at pH 7.0 and 80C over 30 min. KW - gene_fusion KW - multifunctional_enzyme AU - Hong, Su-Young AU - Lee, Jin-Suk AU - Cho, Kye-Man AU - Math, Renukaradhya AU - Kim, Yong-Hee AU - Hong, Sun-Joo AU - Cho, Yong-Un AU - Cho, Soo-Jeong AU - Kim, Hoon AU - Yun, Han-Dae PY - 2007/06/21/ UR - http://dx.doi.org/10.1007/s10529-007-9334-5 ER -

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