Purification and Characterization of Cutinase from<i>Venturia inaequalis</i>

Abstract

K61ler, W., and Parker, D. M. 1989. Purification and characterization of cutinase from Venturia inaequalis. Phytopathology 79:278-283. Venturia inaequalis was grown in a culture medium containing purified cutinase from V. inaequalis is optimal at a pH of 6 and thus different from apple cutin as the sole carbon source. After 8 wk of growth an esterase was the alkaline pH-optimum reported for other purified cutinases. The isolated from the culture fluid and purified to apparent homogeneity. The hydrolysis of the model esterp-nitrophenyl butyrate was less affected by the enzyme hydrolyzed tritiated cutin and thus was identified as cutinase. The pH. The esterase activity was strongly inhibited by diisopropyl purified cutinase is a glycoprotein with a molecular mass of 21-23 kg/ mol, fluorophosphate, and the phosphorylation of one serine was sufficient for as determined by various procedures. Remarkable structural features are a complete inhibition. Thus, cutinase from V. inaequalis belongs to the class high content of glycine, a high content of nonpolar amino acids, two of serine hydrolases, a characterisitic shared with other fungal cutinases. disulfide bridges, and a high degree of hydrophobicity. Cutin hydrolysis by