Purification and partial characterization of a beta-1,3-glucanase secreted by the mycoparasite Stachybotrys elegans
Tweddell, R.J.; Jabaji Hare, S.H.; Goetghebeur, M.; Charest, P.M.; Kermasha, S.
Bioscience Biotechnology and Biochemistry 59(12): 2223-2227
A beta-1,3-glucanase secreted by Stachybotrys elegans, when grown on minimal synthetic medium containing Rhizoctonia solani cell wall fragments, was purified to homogeneity. The purification method involved ammonium sulfate precipitation and ion-exchange and size-exclusion chromatographies. The molecular mass of the enzyme was estimated under denaturing conditions to be about 94 kDa. The enzyme had an optimum pH of 5.0 and was most active between 40 and 50 degree C. Except for Mn-2+, the enzyme activity was not sensitive to the metal ions tested and K-m of 0.18mg/ml was estimated for laminarin as a substrate. Cell wall lytic activity of purified beta-1,3-glucanase was tested on actively growing R. solani hyphae. beta-1,3-Glucanase induced morphological changes such as hyphal tip swelling, bursting, leakage of cytoplasm, and formation of numerous septae.