Purification and characterization of chitinase from Candida albicans.
A novel procedure was used to purify a cytosolic chitinase from Candida albicans to electrophoretic homogeneity. The results represent the first demonstration of the purification of a fungal intracellular chitinase using the criterion of a single band detected following silver-staining of a polyacrylamide gel run under denaturing conditions. Purified chitinase had pH and temperature optima of 5.0 and 50 degrees C, respectively. Inhibition of enzyme activity by allosamidin was pH-dependent occurring maximally at pH 8.0. Phospholipids had similar marked and highly specific effects on the activities of both the purified soluble enzyme and a solubilized microsomal chitinase from C. albicans. Evidence is provided for the existence of a complex chitinolytic system in this organism.
Mellor
K J
KJ
Department of Microbiology, University of Leeds, UK.
Nicholas
R O
RO
Adams
D J
DJ
D002176:Candida albicans / Q000201:enzymology*; D002688:Chitinases / Q000302:isolation & purification*; D002852:Chromatography, Ion Exchange; D006863:Hydrogen-Ion Concentration; D010743:Phospholipids / Q000494:pharmacology
D010743:Phospholipids; D002688:Chitinases