Mellor K J, Nicholas R O, Adams D J
Department of Microbiology, University of Leeds, UK.
FEMS Microbiol Lett. 1994 Jun 1;119(1-2):111-7. doi: 10.1111/j.1574-6968.1994.tb06876.x.
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.
