Purification of the isocitrate lyase extracted from Microbacterium laevaniformans was investigated. The isocitrate lyase was purified 43.6 folds by the following continuous treatment with ammonium sulfate fraction, DEAE-cellulose, DEAE-sephacel and Sephadex G-200 chromatography. The purified isocitrate lyase was showed to be a single protein band by polyacrylamide gel electrophoresis. The molecular weight of the purified isocitrate lyase was estimated 54,000 Da by the SDS-polyacrylamide gel electrophoresis. The Km and Vmax values for isocitrate were estimated to be 0.83mM and 0.33units/㎖, respectively. Activity of isocitrate lyase was inhibited by cystein-HCl and glutathione.

• 서승교(대구산업정보대학 환경관리과) | Seung-Kyo Suh (Dept. of Environmental Management, Taegu Polytechnic College)
• 김정호(경산대학교 환경학부) | Jung-Ho Kim (Fauculty of Environmental Science and Engineering, Kyungsan University)