Analysis of enzyme composition in the spore matrix of Colletotrichum gloeosporioides, causal agent of mango anthracnose.
Weng F. Y., Chuang T. Y.
Author Affiliation: Department of Plant Pathology and Entomology, National Taiwan University, Taipei, Taiwan.
Plant Pathology Bulletin 5 : 181-187
Abstract : C. gloeosporioides [Glomerella cingulata] isolate 5-26, Group II, was used to determine the components of the spore matrix. An SDS-PAGE protein pattern showed that there were protein components in the conidial matrix and that the molecular weight was c. 20-110kDa. The condensed precipitation bands showed at 36-45kDa and 24kDa. Enzyme activities were assayed. Invertase, non-specific esterase and ?-D-glucosidase were detected in the matrix, but cell wall degrading enzymes (polygalacturonase, polygalacturonate transeliminase, polymethyl trans-eliminase and cellulase) were not detected. High invertase activity was detected. Separation of conidial matrix protein components by gel filtration chromatography (GFC) was used to study the protein components of the conidial matrix. Three peaks were obtained after eluting the S-200 sephacryl HR column (based on absorbance at 280 nm). Peak I (PI) contained the total enzyme activities and a high quantity of carbohydrates. It is suggested that PI proteins were glycoproteins. Enzyme activity was not detected in peaks II and III.