| 초록 |
In this study, expression of cold-active lipase from psychrophil Janthinobacterium sp. was carried out. That protein gene encodes 309 amino acids and the expected protien molecular weight is about 37 kDa. The cold-adapted lipase gene was cloned into Escherichia coli DH5. Many overexpression systems cause inclusion body of the target protein. Therefore, we used a weak promoter system trc promoter and obtained a soluble form of lipase. The recombinant lipase was expressed and isolated by Ni2+-NTA affinity chromatography. p-nitrophenol carbonate were used for lipase activity measurement. |
