earticle

영어

It becomes important to develop novel biotechnologies that can subside the global climate change problem, mainly revoked by emission of carbon dioxide (CO2). Since carbonic anhydrase (CA, EC 4.2.1) accelerates the hydration of CO2, CA-based CO2 capture tool is considered as one of the potential systems for solving the problems. Recently, we cloned several types of CAs from marine microalgae or marine bacteria and we re-constructed their sequences optimized for highly-efficient production in E. coli systemThe purpose of this study was to develop a general method for the facile detection of food-borne pathogens. As a proof-of-concept, the fusion proteins containing P1 and P2 domain of Norwalk virus capsid proteins were constructed, expressed and characterized. Recombinant E. coli BL21(DE3) strains harboring pET22-6His-P1 and pET22-6His-P2 were cultivated for the production of fusion proteins. Then, soluble or insoluble fusion proteins were purified in HPLC and measured its binding ability and their secondary structure. The majority of the 6His-P2 fusion proteins were expressed in soluble proteins, while 6His-P1 fusion proteins were expressed in inclusion bodies. After solubilization with urea, 6His-P1 recombinant proteins were further purified by affinity chromatography. A total of 1 mg purified 6His-P2 fusion proteins and 0.7 mg of purified 6His-P1 fusion proteins were obtained with the overall yield from 1 L of bacterial culture. When tested the binding affinity of two fusion proteins in ELISA assay, we observed the 6His-P2 fusion proteins could be used as recognition element for the use of biosensor of food-borne pathogens. Much detailed results will be presented. [This study was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (2011-0010312)]