Arginine Decarboxylase from the pathogenic fungi, Colleotrichum gleosporosides : Purification and Properties

Abstract

Arginine decarboxylase, a polyamine biosynthetic enzyme, was isolated from a phytopathogenic fungi, Colletotrichum gleosporoides, which causes Anthracnose in wide range of plants in many parts ofthe world. The enzyme was purified 25 fold with 16.7% recovery by elution through Sepharose 4B gel column and DEAE Cellulose ion exchange column. As determined by Sepharose 4B gel chromatography, the native molecular mass of the purified enzyme was ~265kDa. SDS-PAGE of the purified enzyme showed two bands around 65 kDa and ~25 kDa, suggesting that possibly this enzyme could be a hexamer of above two sub units. Optimum pH and temperature for the enzyme was 5.2 and 40�C respectively . Beyond 50�C enzyme activity slowly declined and was almost deactivated by 80�C. Approximate Km of the enzyme for the substrate arginine was 67mM.