Skip to main content
ARS Home » Research » Publications at this Location » Publication #185686
Title: CULTURAL CONDITIONS PROMOTING CHITINASE PRODUCTION IN GLIOCLADIUM CATENULATUM

Author
item Kendra, David
item MUHITCH, MICHAEL - ROCHESTER COLLEGE
item Anderson, Amber
item McAlpin, Cesaria

Submitted to: Aflatoxin Workshop
Publication Type: Abstract Only
Publication Acceptance Date: 10/26/2005
Publication Date: 10/26/2005
Citation: Kendra, D.F., Muhitch, M.J., Anderson, A.M., Mcalpin, C.E. 2005. Cultural conditions promoting chitinase production in gliocladium catenulatum. Aflatoxin Workshop.

Interpretive Summary:

Technical Abstract: Gliocladium catenulatum is a known mycoparasite of several fungal genera including Aspergillus and Fusarium. The use of mycoparasites to control fungal plant pathogens either as direct biocontrol agents or as novel sources of antifungal compounds is increasing in importance to serve as environmental alternatives to chemical control. The antagonistic activity of biocontrol agents is attributable to one or more complex mechanisms including the production of antibiotic metabolites, competition for nutrients, induction of systemic acquired resistance, increased nutrient availability to the host plant and production of cell wall hydrolyzing enzymes, including chitinase and beta-1,3-glucanase. Gliocladium catenulatum is known to produce several secondary metabolites with antimicrobial activity, including verticillin and glisoprenin however there is no report of chitinolytic activity. In this paper we report the cultural conditions required to produce chitinase in minimal media supplemented with chitin. Optimal production of extracellular chitinase was observed in a liquid medium previously developed for culturing Fusarium chlamydosporum when cultured at 25 deg C for 21 days and a slightly acidic pH. Chitinase activity was repressed if the colloidal chitin medium was amended with sucrose, glucose, cellulose or starch and eliminated by xylan or lactose. The nitrogen source significantly influenced chitinase activity with KNO2 supporting the best production.