Summary: About 25% of the total cellular invertase and trehalase activity were found in a purified Neurospora wall preparation. Attempts were made to dissociate these enzymes from the walls with chemical reagents and hydrolytic enzymes. A detergent (Triton X-100), a sulphydryl reducing agent (β-mercaptoethanol), a chelating agent (ethylenediaminetetraacetate), a concentrated salt solution (1 M-KCl), and buffers ranging in pH from 3 to 10 did not release them significantly. Snail-gut juice released more than 90% of both enzymes. β-1,3-Glucanase, prepared from WL-12, also released similar amounts. Chitinase released about 80% of invertase and 60% of trehalase. Cellulase did not release any significant amount of either enzyme. Trypsin released only a few per cent of invertase and severely inactivated trehalase. Thus it appears that these two wall-bound enzymes are released only when covalent bonds of the Neurospora wall constituents are disrupted.


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