Constitutive Expression of Arylsulfatase from Pseudoalteromonas carageenovora in E. coli and Its Application to Preparation of Agarose
2007
Kim, M.J. (Dongeui University, Busan, Republic of Korea) | Jang, Y.H. (Dongeui University, Busan, Republic of Korea) | Sung, M.H. (BioLeaders Corp., Daejeon, Republic of Korea) | Kim, Y.H. (Osaka University, Osaka, Japan) | Nam, S.W. (Dongeui University, Busan, Republic of Korea), E-mail: swnam@deu.ac.kr
The arylsulfatase gene (astA, 984 bp ORF) from Pseudoalteromonas carrageenovora genome was amplified by PCR and subcloned into the pHCE-IA vector, in which the hyper consitutive expression (HCE) promoter from the D-amino acid aminotransferase (D-AAT) gene of Geobacillus toevii was employed. The transformant cell, Escherichia coli BL21 (DE3)/pHCE-AST, on LB agar plate containig 4-methylumbelliferyl sulfate, showed an intense fluorescence at 360 nm, indicating that 4-methylumbelliferone was liberated by desulfatate activity. When BL21 (DE3)/pHCE-AST was grown on LB media containing 0.4% glucose or 0.4% glycerol, the arylsulfatase activity was higher at glycerol rather than at glucose.
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