Abstract
An extracellular chitinase of Acremonium obclavatum was partially purified. It had an M r of 45 kDa on SDS-PAGE, and was optimally active at pH 3 to 4 and 50°C. Hg and Mn (10 mM) inhibited activity. The chitinase hydrolysed colloidal chitin more rapidly than crude chitin or isolated A. obclavatum cell walls. The partially-purified enzyme inhibited uredospore germination and germ-tube growth of Puccinia arachidis.
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