Cloning and Characterization of a Bifunctional Cellulase-Chitosanase Gene from Bacillus lichenformis NBL420

  • HONG, IN-PYO (School of biotechnology and Bioengineering Kangwon National University) ;
  • HONG-KI JANG (School of biotechnology and Bioengineering Kangwon National University) ;
  • SHIN-YOUNG LEE (School of biotechnology and Bioengineering Kangwon National University) ;
  • SHIN-GEON CHOI (School of biotechnology and Bioengineering Kangwon National University)
  • Published : 2003.02.01

Abstract

A 1,3 kb cellulase gene encoding novel bifunctional cellulase-chitosanase activity was cloned from biopolymer-producing alkali-tolerant B. lichenformis NBL420 in E. coli. A recombinant cellulase-chitosanase, named CelA, was expressed and purified to homogeneity. The activity staining and the enzymatic characterization of the purified CeIA revealed bifunctional activities on carboxymethyl cellulose (CMC) and glycol-chitosan. The similar characteristics of the enzymatic activities at the optimum pH, optimum temperature, and thermostability Indicated that CelA used a common catalytic domain with relaxed substrate specificity. A comparison of the deduced amino acids in the N-terminal region revealed that the mature CelA had a high homology with the previously identified bifunctional cellulase-chitosanase of Myxobacter sp. AL- 1.

Keywords

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