Partial purification and properties of extracellular chitinase produced by Acremonium obclavatum, an antagonist to the groundnut rust, Puccinia arachidis.

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.