Purification and characterization of two isozymes of polygalacturonase from Botrytis cinerea. Effect of calcium ions on polygalacturonase activity.
The phytopathogenic fungus Botrytis cinerea produces a set of polygalacturonases (PGs) which are involved in the enzymatic degradation of pectin during plant tissue infection. Two polygalacturonases secreted by B. cinerea in seven-day-old liquid culture were purified to apparent homogeneity by chromatography. PG I was an exopolygalacturonase of molecular weight 65 kDa and pI 8.0 and PG II was an endopolygalacturonase of 52 kDa and pI 7.8. Enzymatic activity of PG I and PG II was partially inhibited by 1 mM CaCl2, probably by calcium chelation of polygalacturonic acid, the substrate of the enzyme.
Cabanne
Charlotte
C
Laboratoire de Biochimie Végétale Appliquée, Universite V. Segalen Bordeaux 2/INRA, Faculté d'oenologie, Talence, France.
Donèche
Bernard
B
D020171:Botrytis / Q000201:enzymology*; D002122:Calcium Chloride / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D010368:Pectins / Q000378:metabolism; D011096:Polygalacturonase / Q000187:drug effects / Q000302:isolation & purification* / Q000378:metabolism
D007527:Isoenzymes; D010368:Pectins; D011096:Polygalacturonase; D002122:Calcium Chloride; C003181:polygalacturonic acid