Release of Wall - bound Invertase and Trehalase in Neuruspura crassa by Hydrolytic Enzymes By PATRICIA

About 25 yo 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-IOO), a sulphydryl reducing agent (P-mercaptoethanol), a chelating agent (ethylenediaminetetraacetate), a concentrated salt solution (I 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. /?-I ~-Glucanase, prepared from Bacillus circulans WL-12, also released similar amounts. Chitinase released about 80 yo of invertase and 60 yo 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.