Abstract
Debaromyces cantarellii Capriotti contains an inulinase activity which is inducible by growth on inulin but not on other β-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 β-fructofuranosidase with a specificity partly overlapping with that of the inulinase(s).
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Beluche, I., Guiraud, J.P. & Galzy, P. Inulinase activity ofDebaromyces cantarellii . Folia Microbiol 25, 32–39 (1980). https://doi.org/10.1007/BF02876395
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DOI: https://doi.org/10.1007/BF02876395