Purification and characterization of two isozymes of polygalacturonase from Botrytis cinerea.: Effect of calcium ions on polygalacturonase activity

被引:36
作者
Cabanne, C [1 ]
Donèche, B [1 ]
机构
[1] Univ Bordeaux 2, Lab Biochim Vegetale Appl, Fac Oenol, INRA, F-33405 Talence, France
关键词
Botrytis cinerea; polygalacturonase; calcium; pectin;
D O I
10.1078/0944-5013-00147
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:183 / 189
页数:7
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