FUNCTIONAL EXPRESSION OF A BACILLUS LICHENIFORMIS LACCASE IN E. COLI ROSETTA 2 AND E.COLI ROSETTA BLUE STRAINSPallavi Jaiswal and Pallavi Mittal
Rosetta host strains are designed to enhance the expression of eukaryotic proteins that contain codons rarely used in E. coli Laccasegene from Bacillus licheniformis was cloned and expressed in E. coli Rosetta2 and Rosetta blue strain under the control of T7 promoter. The molecular weight of expressed laccase was observed to be 65KDa. It was observed that expression of laccase protein was very low in E.coli Rosetta blue strain as compared to E.coli Rosetta2 strain. Thus laccase gene from Bacillus licheniformis can be expressed efficiently in E.coli Rosetta 2 strain. Laccases belong to the multi-copper oxidase (MCO) enzyme family. These enzymes are classified as blue copper proteins and contain between one and six copper atoms. They are produced by various fungi, plants, insects and bacteria. Numerous studies have shown that laccase catalyzed decolorization of textile dyes. To date, only fungal laccases are industrially relevant for the detoxification of synthetic dyes and other applications owing to their higher redox potential compared to bacterial laccases. However, more recently bacterial laccases have also been shown to successfully oxidize dyes in the presence and absence of redox mediators. Developing bacterial laccases for biotechnological applications will be advantageous because they are sustainable and can be produced in a short time in inexpensive media.
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