The degradation of hemicelluloses is an early event in wood decay by brown-rot fungi. An understanding of the physical properties of hemicellulases may suggest target mechanisms for the development of new control agents. Endo-b-1,4-xylanase was partially purified by column chromatography from wood decayed by Postia (= Poria) placenta. The enzyme was extremely resistant to denaturing conditions; no loss of activity was detected after 2 h in 9 M urea or 6 M guanidine-HCl. Boiling the enzyme for 5 min in 2.5% SDS + 0.5% b-mercaptoethanol reduced its activity by 65%, as measured by the production of reducing sugars. The activity of a-D-galactosidase, another enzyme detected in large quantities in the decayed wood, was reduced by 98% under these conditions. Optimum pH and temperature ranges were pH 2-6 and 50-60°C, respectively. The enzyme appears to be a glycoprotein containing 50-60% carbohydrate (w/w); the carbohydrate moiety may protect the enzyme from adverse environmental conditions. The control of brown rot by in situ inactivation of xylanase may not be feasible because of the enzyme's extreme stability.

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