원문정보
초록
영어
A novel lipolytic enzyme was isolated from a metagenomic library after demonstration of lipolytic activity on an LB agar plate containing 1% (w/v) tributyrin. A novel esterase gene (estIM1), encoding a lipolytic enzyme (EstIM1), was cloned using a shotgun method from a pFosEstIM1 clone of the metagenomic library, and the enzyme was characterized. The deduced amino acid sequence was 62% identical to that of an esterase from an uncultured bacterium (ABQ11271). EstIM1 was active over a temperature range of 1-50ºC, at alkaline pH. The activation energy for hydrolysis of p-nitrophenyl propionate was 1.04 kcal/mol, within a temperature range of 1-40ºC. The activity of EstIM1 was about 60% of maximal even at 1ºC, suggesting that EstIM1 is efficiently cold-adapted. Further characterization indicated that the esterase may be very valuable in industrial applications. (This work was supported by a HTS-based Integrated Technology Development grant and by Basic Science Research Program from the MEST.)