BMB Reports
- Volume 31 Issue 1
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- Pages.53-57
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- 1998
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- 1976-670X(eISSN)
Expression and Characterization of CMCax Having β-1,4-Endoglucanase Activity from Acetobacter xylinum
- Koo, Hyun-Min (Department of Biochemistry, College of Science and Bioproducts Research Center, Yonsei University) ;
- Song, Sung-Hee (Department of Biochemistry, College of Science and Bioproducts Research Center, Yonsei University) ;
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Pyun, Yu-Ryang
(Department of Biochemistry, College of Science and Bioproducts Research Center, Yonsei University) ;
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Kim, Yu-Sam
(Department of Biochemistry, College of Science and Bioproducts Research Center, Yonsei University)
- Published : 1998.01.31
Abstract
The CMCax gene from Acetobacter xylinum ATCC 23769 was cloned and expressed in E. coli. With this gene, three gene products - mature CMCax, CMCax containing signal peptide(pre-CMCax), and a glutathione-S-transferase(GST)-CMCax fusion enzyme - were expressed. CMCax and pre-CMCax are aggregated to multimeric forms which showed high CMC hydrolysis activity, whereas GST-CMCax was less aggregated and showed lower activity, indicating that oligomerization of CMCax controbutes to the cellulose hydrolysis activity to achieve greater efficiency. The enzyme was identified to be an