Bacillus sp. LJ-25가 생성하는 extracellular chitinase의 정제 및 특성 = Purification and Some Proprties of the Extracellular Chitinase from Bacillus sp. LJ-25

다국어 초록 (Multilingual Abstract)

The extracellular chitinase from Bacillus sp. LJ-25 was pruified Sephadex G-100 gel filtration, DEAE-Cellulose and CM-Spephadex C25 column chromatography. The pruified chitinase showed a single band on disc and SDS polyacrylamide gel electrophoresis and the molecular weight was estimated to be about 50KDa. The Optimum pH and temperature for the activity of the purified extracellular chitinase were 7.5 and 35℃, respectively. The activity of chitinase was strongly inhibited by metal ions such as Zn²+, Ba²+, Co²+, Mn²+ and Cu²+. The purified chitinase did not hydrolyze N,N??-diacetylchitobiose, N,N, N'-triacetylchitotriose and p-nitrophenol-N-acetyl-β-D-glucosaminide, which are known to be the substrates of exo-type chitinase. The products in hydolysis of colloidal chitin with the chitinase were N-acetylglucosamine, N,N'-diacetylchitobiose and N,N,N'-triacetylchitotriose.