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Evaluation of Antifungal Activity of Purified Chitinase 42 from Trichoderma atroviride PTCC5220

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Author(s): M.J. Harighi | M.R. Zamani | M. Motallebi

Journal: Biotechnology
ISSN 1682-296X

Volume: 6;
Issue: 1;
Start page: 28;
Date: 2007;
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Keywords: Trichoderma atroviride | chitinase | antifungal activity | ion-exchange chromatography

ABSTRACT
Chitin, a linear polymer of N-acetylglucosamine residues, has been the most abundant polymer in nature after cellulose. It plays a major role in fungal cell walls. Chitinase enzymes degrade the polymer into its component residues by breaking the β-1,4 glycosidic bonds. As a producer of a variety of chitinase enzymes, the filamentous fungus, Trichoderma, has become an important means of biological control for fungal diseases. Chitinase 42 kDa (Chit42) was purified from supernatants of T. atroviride, an over producer of chitinase enzyme, grown in medium supplemented with colloidal chitin as the sole carbon source. Enzyme purification was achived in two steps ion exchange chromatography using CM-Sepharose and DEAE- Sepharose. The purity of Chit42 was investigated by SDS-PAGE. The results showed one band about 42 kDa after the second step of chromatography which showed chitinase activity in enzyme assay technique. This purified Chit42 has shown to have inhibitory activity on mycelial growth and also, in vitro lytic activity on cell wall of Rhizoctonia solani (AG2-2), causal agent of root rot in sugar beet. The purified Chit42 was optimally active at pH 5 and at 40°C. It is thermally stable at 60°C for more than 240 min at pH 5.

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