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Microbiology 144 (1998), 1575-1581
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microbiology, Vol 144, 1575-1581, Copyright © 1998 by Society for General Microbiology

ARTICLES

Inducible chitinolytic system of Aspergillus fumigatus

GM Escott, VM Hearn and DJ Adams
Department of Microbiology, University of Leeds, UK.

Incubation of Aspergillus fumigatus NCPF 2140 in growth medium containing 1% chitin as sole carbon source led to induction of specific extracellular chitinolytic activity of 1.5 mumol GlcNAc released min-1 (mg protein)-1. The effect was repressed by the inclusion of GlcNAc in the medium, indicating regulation by a negative feedback mechanism. Extracellular chitinase activity was inhibited by allosamidin (IC50 0.12 microM). Multiple chitinolytic enzymes were detected on zymograms of extracellular preparations; levels of individual enzymes induced were dependent upon whether cells were incubated with purified colloidal chitin or a crude preparation of crystalline chitin. A major, inducible, 45 kDa chitinase was purified using ammonium sulphate precipitation, chitin affinity chromatography and a novel procedure involving the electroelution of the enzyme from a substrate gel containing glycol chitin. The enzyme is a glycoprotein with endochitinase activity.


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A. K. Jaques, T. Fukamizo, D. Hall, R. C. Barton, G. M. Escott, T. Parkinson, C. A. Hitchcock, and D. J. Adams
Disruption of the gene encoding the ChiB1 chitinase of Aspergillus fumigatus and characterization of a recombinant gene product
Microbiology, October 1, 2003; 149(10): 2931 - 2939.
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