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Properties of extracellular chitinase from Myrothecium verrucaria, an antagonist to the groundnut rust Puccinia arachidis

Govindsamy, V., Gunaratna, K.R., Balasubramanian, R.
Canadian journal of plant pathology 1998 v.20 no.1 pp. 62-68
Myrothecium verrucaria, Puccinia arachidis, chitinase, fungal antagonists, enzyme activity, molecular weight, chitin, temperature, pH, enzyme inhibitors, zinc sulfate, calcium chloride, Hypocrea lixii, lysozyme, spore germination, fungal spores
An extracellular chitinase activity was detected from Myrothecium verrucaria, an antagonist of the groundnut rust fungus Puccinia arachidis, and chitinase was purified using ammonium sulphate precipitation and Sephadex G-100 gel chromatography. On sodium dodecyl sulfate polyacrylamide gels, the purified chitinase migrated as a single band of molecular mass of 40 kDa. Commercial chitin powder and colloidal chitin were the preferred substrates for the purified chitinase. The chitinase showed broad pH (3.5 to 7.5) and temperature (35 degree to 55 degree C) optima, and the metal salts ZnSO4 and CaCl2 inhibited chitinase activity. The purified enzyme inhibited the growth of Trichoderma harzianum and urediniospore germination of P. arachidis; it also contained a lysozyme activity that was inhibited by histamine and N-acetylglucosamine.