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Expression, Purification and Characterization of Recombinant Serratia Marcescens Nuclease

Author: CaiJunJie
Tutor: LiRongXiu；ZhangGaoXia
School: Shanghai Jiaotong University
Course: Biological Engineering
Keywords: Serratia marcescens nuclease gene construction protein expression biology activity
CLC: Q78
Type: Master's thesis
Year: 2011
Downloads: 45
Quote: 0
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Abstract


The expression gene of Serratia marcescens nuclease (strain SM6) is constructed to vector SMnucA-p ET43.1a according to the amino acid sequence. The expression vector SMnucA-p ET43.1a is transformed into E. coli BL21 (DE3) and SMnucA protein is expressed as inclusion bodies under IPTG induction. After purification, the enzyme is refolded. It is shown in the SDS-PAGE analysis that the relative molecular mass of SMnucA is 26 kD which is consistent with the theoretical predicted weight. The enzymatic activity of the refolded Serratia marcescens nuclease is confirmed through DNA degradation experiment. The enzymatic activity is consistant with that in the publication.

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CLC: > Biological Sciences > Molecular Biology > Genetic engineering (genetic engineering)
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