| 초록 |
Functional expression of recombinant protein is a constant issue in diverse fields of biotechnology. In this study, using advanatage of cell-free protein synthesis, we developed a method to study the effect of molecular chaperones on the functional synthesis of recombinant proteins. After the synthesis of a series of molecular chaperones, the reaction mixture for cell-free protein synthesis was reprogrammed for synthesis of Candida antarctica lipase B (CalB). The effect of a pre-synthesized molecular chaperone on protein folding was determined by measuring the enzymatic activity of CalB synthesized in the second reaction. We believe that the brilliant method can be very helpful for expression of recombinant protein in a difficult situation because of lack of folding reagent. |
