Experiments designed to compare the degree of localization of the cellulase enzymes of some white, brown and soft rot organisms are described. The site and nature of binding of the enzymes is discussed. The technique is ellution of mycelium grown in liquid culture with a variety: of agents including acetate buffer, carboxymethyl cellulose solution, borate/glycerol buffer and urea. The mycelium was assayed for cellulase activity before and after washing. Eluted protein was also assayed. The effect on retention of cellulases of treatment with a (1,3) ß glucanase was determined. Brown rot organisms showed a far lower retention of cellulases to the mycelium than the soft and white rot organismns. Carboxymethylcellulose solution was found to be only slightly effective as a protein eluent on the white and soft rot organisms indicating low substrate affinity. 8 M urea was found to be an effective protein eluting agent - possibly implying hydrogen bonding between cellulases and the fungus. Borate/glycerol buffer was also shown to be an effective agent for protein elution - however· less so than urea. This agent probably binds to carbohydrates, either glycoprotein enzymes or binding sites on the organism, thius displacing protein. (1,3) ß glucanase markedly decreased the retention of cellulase activity in soft and white rot organisms indicating binding to a (1,3) ß glucan. It is postulated that cellulase retention mechanisms found in soft and white rot organisms and absent from brown rots have a significant role in the production of the characteristic observed patterns of decay of the three types.

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