PRODUCTION OF CHITINASE FROM BIOCONTROL AGENTS: Trichoderma spp. | ||||
| Journal of Soil Sciences and Agricultural Engineering | ||||
| Article 7, Volume 29, Issue 10, October 2004, Page 6025-6036 PDF (3.26 MB) | ||||
| Document Type: Original Article | ||||
| DOI: 10.21608/jssae.2004.243883 | ||||
 View on SCiNiTO | ||||
| Author | ||||
| H. M. Hassan, | ||||
| Microbial Chemistry Dept., National Research Centre Dokki, Cairo, Egypt | ||||
| Abstract | ||||
| Trichoderma spp. play an important role in the destruction of plant pathogenic fungi, and were found to produce chitinase, which hydrolyzes chitin, a major component of many pathogenic fungi cell walls. Out of four Trichoderma isolates, Trichoderma harzianum T3 and T4 strains showed high chitinolytic activity on chitin - basel agar medium. Factors involved the production of chitinase were investigated. Maximum enzyme levels of ( 10 t015.9 U I ml) were achieved after six days incubation at 28°C and initial pH of medium 6.5 The enzyme was produced only in the presence of colloidal chitin at a concentration of 1 % (w/v) , as a sole carbon source, suggesting the inducible nature of the enzyme. Trichoderma harzianum T 4 was found to be very efficient to lyse mycelia of Microphomina phaseolina, Rhizoctonia solani and Sclerotium rolfsii. Partial purification of chitinase from Trichoderma harzianum T4 was achieved by (NH4)2 S04 precipitation followed by gel filtration using Sephadex G - 200. The partially purified enzyme was found to be highly active at pH 6.5 and 50°C, and thermostable at 50°C for 60 min. Mn2+ , Ca2+ and Fe2+ activated the enzyme, whereas C02+ , Cu2+ , Zn2+ and Hg2+ had different inhibitory effects. | ||||
| Keywords | ||||
| Trichoderma; biological control; chitinase; partial purification; enzyme properties | ||||
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