원문정보
초록
영어
Recently, the freezing-intolerant Antarctic springtail is known to have various carbohydrases to digest the ingested food in the cold environment. Previously, we succeeded production of endogenous GHs of antartic springtail in E.coli, but it has not been accomplished mass production. Here, we report the successful mass production, purification, and characterization of C. antaricticus cellulase (CaCEL), laminarinase (CaLAM), and mannanase (CaMAN) using B. mori as host. In B. mori expression system, three GHs were detected solubilized proteins. Active three GHs were purified to near 90% purity from haemolymph and fatbody lysate by desalting chromatography and anion exchange chromatography. The yield of GHs produced by B. mori was estimated at each over 67 mg/L, significantly similar that of the GHs form E. coli (about 0.69 mg/L). Additionally, the specific activity of GHs from B. mori was highly than that form E. coli (about each 0.8 U/mg versus 3.4 U/mg). These results indicated B. mori was a convenient expression system for the efficient production of GHs. *This work was supported by the Bio-industry Technology Development Program, Ministry for Food, Agriculture, Forestry and Fisheries, Republic of Korea (No: 111062-03-1-HD110).