Purification and characterization of a pectate lyase from Fusarium oxysporum f.sp. lycopersici produced on tomato vascular tissue
1996
The tomato vascular wilt pathogen Fusarium oxysporum f.sp. lycopersici produced pectate lyase (PL; EC 4.2.2.2.) activity when grown on polygalacturonic acid (PGA) and on tomato vascular tissue as the sole carbon sources. A PL was purified to apparent homogeneity by preparative isoelectric focussing. The enzyme had an approximate mol. Wt. of 25 kDa as determined by SDS PAGE. The pI of the PL was 8.7, and pH and temperature optima for enzyme activity were 9.0 and 42 degrees C, respectively. PL was active as a monomer, hydrolyzed PGA in an endo-manner, and exhibited an absolute requirement for calcium. Absence of extracellular PL after treatment with tunicamycin indicated that N-glycosylation of the enzyme was essential for secretion. Sequencing of 12 N-terminal amino acids showed 100% homology to an endo-PL from Fusarium solani f.sp. pisi.
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