alexa Purification and partial characterization of two chitinases from the mycoparasitic fungus Talaromyces flavus.


Journal of Microbial & Biochemical Technology

Author(s): DuoChuan LI, Chen S, Jing LU

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Abstract Chitinases were produced by Talaromyces flavus CGMCC 3.4301 when it was grown in the presence of chitin. Two chitinases from the culture filtrate of T. flavus were purified to homogeneity by fractional ammonium sulphate precipitation, ion-exchange chromatography on DEAE-Sepharose and Phenyl-Sepharose hydrophobic interaction chromatography. By SDS-PAGE, the molecular weight of the two enzymes was estimated to be 41 and 32 kDa, respectively. The 41 kDa chitinase (CHIT41) had a 4.0 pH optimum; the 32 kDa chitinase (CHIT32) optimum activity was at pH 5.0. The optimum temperature for the two chitinase activities was 40 degrees C. The two chitinases had activity against cell wall of Verticillium dahliae, Sclerotinia sclerotiorum and Rhizoctonia solani, and inhibited spore germination and germ tube elongation of Alternaria alternata, Fusarium moniliforme, and Magnaporthe grisea. This article was published in Mycopathologia and referenced in Journal of Microbial & Biochemical Technology

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