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Received October 30, 2010
Accepted November 18, 2010
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Constitutive overexpression of Pseudoalteromonas carrageenovora arylsulfatase in E. coli fed-batch culture
1Department of Biomaterial Control, Dong-Eui University, Busan 614-714, Korea 2Department of Biotechnology and Bioengineering, Blue-Bio Industry RIC, Dong-Eui University, Busan 614-714, Korea
swnam@deu.ac.kr
Korean Journal of Chemical Engineering, April 2011, 28(4), 1101-1104(4), 10.1007/s11814-010-0488-9
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Abstract
The arylsulf atase gene (astA) from Pseudoalteromonas carrageenovora genome was subcloned into pHCEIA vector, in which the hyper constitutive expression (HCE) promoter from the D-amino acid aminotransferase (DAAT) gene of Geobacillus toebii was employed. When the constructed pHCE-AST was introduced into E. coli, the transformant showed the hydrolyzing activity for 4-methylumbelliferyl-sulfate and p-nitrophenyl-sulfate. When the cell was cultured on fermentor containing MaxyBroth-HD medium with 1% glycerol, the enzyme activity reached 12.8unit/mL. On MaxyBroth-HD medium with 2% glycerol, the cell showed 2.7-fold higher arylsulfatase expression than that with 1% glycerol. The fed-batch cultivation employing MaxyBroth-HD medium and additional feeding of glycerol gave about 143 unit/mL of arylsulfatase at 20 h, which corresponds to 4-fold higher enzyme activity than that of 2% glycerol batch culture. Most of arylsulfatase activity in fed-batch culture was produced in the extracellular medium, whereas the activity in the batch cultures was localized in the periplasmic cell space.
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