Inulinase activity of Debaromyces cantarellii.
Debaromyces cantarellii Capriotti contains an inulinase activity which is inducible by growth on inulin but not on other beta-fructosides. The induction is inhibited by glucose and fructose. The system is situated in the cell wall and can be best extracted with a 20 mM phosphate buffer at pH 8.5. The inulinase activity shows pH optima at 4 and 6, suggesting the presence of two enzymes, the latter being more tightly bound to the cell wall. Both enzymes degrade inulin from the nonreducin end. The cells also contain a constitutive beta-fructofuranosidase with a specificity partly overlapping with that of the inulinase(s).
D001203:Ascomycota / Q000201:enzymology*; D002473:Cell Wall / Q000201:enzymology; D004790:Enzyme Induction; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007444:Inulin / Q000378:metabolism; D004718:Saccharomycetales / Q000201:enzymology* / Q000648:ultrastructure; D013379:Substrate Specificity; D013696:Temperature
D007444:Inulin; D006026:Glycoside Hydrolases