Bacillus stearothermophilus의 mutant가 생산하는 cyclodextrin glucanotransferase(CGTase)를 affinity chromatography법을 이용하여 정제하였다. 이 CGTase의 회수율은 95%이었고 specific activity는 26.2U/mg protein에서 485.5U/mg protein으로 증가하였다. 정제된 CGTase는 SDS-polyacrylamide gel 전기영동 결과 단일 band로 나타났다. CGTase는 affinity chromatography를 이용하여 one-step으로 정제할 수 있었다.
- The cyclodextrin glucanotransferase (CGTase) of a mutant of Bacillus stearothermophilus was purified in one step by affinity chromatography. The recovery was 95%. The specific activity of the CGTase increased from 26.2 U/mg protein to 485.5 U/mg protein. The purified CGTase was almost homogeneous by SDS-polyacrylamide gel electrophoresis. The one-step purification proved to be feasible with the mutant in contrast to the parent strain, which required pre-purification step of ammonium sulfate precipitation.
