1887

Abstract

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 of 3·9 mg chitin ml [17·6 m--acetylglucosamine (GlcNAc) equivalents] and of 23 nmol GlcNAc formed min (mg protein). The potential of the streptomycete antibiotic allosamidin as an antifungal agent is discussed in view of its dose-dependent inhibition of chitinase activity (IC = 0·3 μ). Allosamidin was a potent competitive inhibitor of enzyme activity ( = 02·3 μ).

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/content/journal/micro/10.1099/00221287-135-6-1417
1989-06-01
2021-10-28
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