BASIC XYLANASES FROM THE FUNGAL TOMATO PATHOGEN FUSARIUM英文资料.pdfVIP

Journal of Plant Pathology (2001), 83 (1), 27-36 Edizioni ETS Pisa, 2001 27 BASIC XYLANASES FROM THE FUNGAL TOMATO PATHOGEN FUSARIUM OXYSPORUM F.SP. LYCOPERSICI F. Cardinale and A. Matta Di.Va.P.R.A., Università degli Studi di Torino, Via Leonardo da Vinci 44, I-10095 Grugliasco (Torino), Italy ABSTRACT play a prominent role in typically non-lytic diseases. Among them, pectin-degrading enzymes are the best We purified four xylan-degrading enzymes (endo-xy- studied by far, as related to fungal pathogenesis (for a lanases: EC 3.2.1.8) produced in vitro by the fungal review, see Alghisi and Favaron, 1995). pathogen Fusarium oxysporum f.sp. lycopersici (Fol). Several lines of evidence suggest however that hemi- The xylanases were resolved by a combination of ion cellulases (notably endo-xylanases, EC 3.2.1.8) may be exchange and hydrophobic interaction chromatogra- significant in plant-pathogen interactions. They are not phy, and preparative nativeelectrophoresis. able to macerate tissues by themselves, especially in di- They had molecular masses of 38, 34, 22 and 19 kDa, cotyledons, where xylan polymers are much less abun- pI higher than 9.3, endo-cleavage mechanism and maxi- dant than in the cell wall of monocotyledons. These en- mal activity at pH 6.0 and 45°C. Comparison of the re- zymes may not be massively produced in interactions action products showed differences in the cleavage between the dicots and their pathogens (Holden and