Cyclodextrin Glucanotransferase from Bacillus stearothermophilus:Purification by Affinity Chromatography and Its Properties

Bacillus stearothermophilus가 생산하는 Cyclodextrin Glucanotransferase: Affinity Chromatography를 이용한 정제 및 성질

  • 안중훈 (한국식품개발연구원) ;
  • 황진봉 (한국식품개발연구원) ;
  • 김승호 (한국식품개발연구원)
  • Published : 1990.12.01

Abstract

The cyclodextrin glucanotransferase (CGTase) was purified from the culture broth of Bacillus stearothermophilus by ammonium sulfate precipitation and affinity chromatography. The specific activity of the CGTase increased by about 31-fold from 111.5 U/mg protein to 3445.0 Ulmg protein. The SDSPAGE indicated that the purified CGTase was homogeneous and the molecular weight of the purified CGTase was about 78,000. The optimum pH and temperature was 6.0 and $60^{\circ}C$, respectively. This enzyme was stable from pH 5.5-10.0. The enzyme retained its full activity at the incubation temperature up to $60^{\circ}C$ and calcium ion increased the thermal stability. The isoelectric point was about 4.8.

Keywords

Bacillus stearothermophilus;cyclodextrin glucanotransferase;affinity chromatography