[Purification and properties of chitinase from Enterobacter aerogenes].
A bacterium producing chitinase was isolated from the dead body of Gymephorap ruoergensis. A chitinase was isolated from the culture of E. aerogenes and purified by means of ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Sephadex G-100 column gel filtration. The purified chitinase showed homogeneity on the native polyacrylamide gel electrophoresis. Its molecular weight was estimated to be about 42.5 kD by SDS-PAGE. The optimum pH and temperature for hydrolysis of chitin were 6.0 and 55 degrees C respectively. Michaelis constant was 2.88 mg/mL. Different metal ions showed different effects on the chitinase activity, The chitinase activity was enhanced by Zn2+, Ba2+, Ca2+, Mn2+ and was strongly inhibited by Hg2+, Co2+, Mg2+.
Tang
Y
Y
National Laboratory of Grassland Biological Control, Sichuan University, Chengdu 610064.
Zhao
J
J
Ding
S
S
Liu
S
S
Yang
Z
Z
D000818:Animals; D002688:Chitinases / Q000737:chemistry / Q000302:isolation & purification*; D021902:Enterobacter aerogenes / Q000201:enzymology* / Q000302:isolation & purification; D004795:Enzyme Stability / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D007915:Lepidoptera / Q000382:microbiology*; D008628:Mercury / Q000494:pharmacology; D013696:Temperature; D015032:Zinc / Q000494:pharmacology
D002688:Chitinases; D008628:Mercury; D015032:Zinc