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Candida albicans chitinase isolated using the Dyno-Mill disruption technique was characterized using an improved radiometric assay procedure. The enzyme had apparent temperature and pH optima of 45 °C and 65, respectively. The preparation yielded an apparent K m of 3·9 mg chitin ml−1 [17·6 mm-N-acetylglucosamine (GlcNAc) equivalents] and V of 23 nmol GlcNAc formed min−1 (mg protein)−1. The potential of the streptomycete antibiotic allosamidin as an antifungal agent is discussed in view of its dose-dependent inhibition of C. albicans chitinase activity (IC50 = 0·3 μm). Allosamidin was a potent competitive inhibitor of enzyme activity (K i = 02·3 μm).
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