%0 Journal Article %A Chang, Patricia L. Y. %A Trevithick, J. R. %T Release of Wall-bound Invertase and Trehalase in Neurospora crassa by Hydrolytic Enzymes %D 1972 %J Microbiology, %V 70 %N 1 %P 13-22 %@ 1465-2080 %R https://doi.org/10.1099/00221287-70-1-13 %I Microbiology Society, %X 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 Bacillus circulans 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. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-70-1-13