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KMID : 1007519990080040276
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Food Science and Biotechnology
1999 Volume.8 No. 4 p.276 ~ p.279
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Enhancement of Solubility of Bacillus macerans Cyclodextrin Glucanotrans - ferase By Thioredoxin Fusion
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HAN NAM-SOO
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Abstract
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The E. coli thioredoxin gene (trxA) was used as a gene fusion partner of Bacillus macerans cyclodextrin glucanotransferase (CGTase) gene (cgt) due to its high solubility and modest size. E. coli cells were transformed with the plasmid vector containing trxA-cgt fusion DNA and bacteriophage lambda pL promoter. The thioredoxin-CGTase fusion protein was expressed in E. coli cells at 30℃ by induction with tryptophan, and its concentration in the soluble extract of the cells was measured by a competitive ELISA using anti-CGTase antibody. For 6 hours after induction, the production rate of soluble fusion protein was 87 ㎍·mL^(-1)·hr^(-1), which was over 4 times faster than control CGTase (20 ㎍·mL^(-1)·hr^(-1), revealing the effectiveness of the thioredoxin fusion system on solubilization of CGTase in E. coli.
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