Mechanisms of protection of trehalase against heat inactivation in Neurospora.
The half-life of trehalase and invertase at 65 and 60 C was found to be much greater when intact ascospores of Neurospora tetrasperma were heated, as compared with extracts. By contrast, no protection was afforded these enzymes when they were heated in intact conidia and mycelium of N. crassa or N. tetrasperma. The protective effect of ascospores for trehalase was further investigated by heating ascospore extracts before and after dialysis. The removal of small molecules by dialysis lowered the heat resistance of trehalase significantly in such extracts. When the dialysate from extracts of mycelium, conidia, or ascospores was added to dialyzed enzyme extracts, that from ascospores was by far the most active. However, the same dialysates had only a small protective effect on invertase. The addition of ashed dialysates did not protect trehalase, and trehalose and glucose protected less effectively than the dialysate.
D003956:Dialysis; D004187:Disaccharides / Q000494:pharmacology; D005947:Glucose / Q000494:pharmacology; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006358:Hot Temperature; D009491:Neurospora / Q000201:enzymology*; D013170:Spores / Q000201:enzymology
D004187:Disaccharides; D006026:Glycoside Hydrolases; D005947:Glucose