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Evaluation of a novel bifunctional xylanase-cellulase constructed by gene fusion
- Authors
- An, J.M.; Kim, Y.K.; Lim, W.J.; Hong, S.Y.; An, C.L.; Shin, E.C.; Cho, K.M.; Choi, B.R.; Kang, J.M.; Lee, S.M.; Kim, H.; Yun, H.D.
- Issue Date
- 2005
- Publisher
- Elsevier Inc.
- Keywords
- Bifunctional enzyme; Cellulase; Gene fusion; Xylanase
- Citation
- Enzyme and Microbial Technology, v.36, no.7, pp 989 - 995
- Pages
- 7
- Indexed
- SCOPUS
- Journal Title
- Enzyme and Microbial Technology
- Volume
- 36
- Number
- 7
- Start Page
- 989
- End Page
- 995
- ISSN
- 0141-0229
1879-0909
- Abstract
- An artificial bifunctional enzyme, xylanase-cellulase, has been prepared by gene fusion. Three chimeric genes were constructed that encoded fusion proteins of different lengths. The fusion proteins exhibited both xylanase (XynX) and cellulase (Cel5Z::Ω) activity when cel5Z::Ω was fused downstream of xynX, but not when xynX was fused downstream of cel5Z::Ω. Activities of bifunctional enzymes decreased when a shorter xylanase peptide was fused. Three fusion enzymes were purified, and the molecular weights of the enzymes were estimated by CMC-SDS-PAGE and XYN-SDS-PAGE to be 149, 129, and 87 kDa, respectively. The fusion enzymes displayed optimum cellulase activity at pH 8.0 and 50°C and optimum xylanase activity at pH 8.0 and 70°C. ? 2005 Published by Elsevier Inc.
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