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- W2740240183 abstract "The &fructofuranosidase from Kluyverornyces fragilis was purified to one band on electrophoresis by 3 different methods. Two of the preparations were found to be impure by isoelectric focusing. This demonstrates the need for more than one criteria of homogeneity when purifying this enzyme. The enzyme was found to be a glycoprotein, stable at 5O”C, with a pH optimum of 4.5. The cations Hg”+, Ag+, Cu2+ and Cd’+ exhibited a marked inhibition of the enzyme. Competitive inhibition was observed with the fructose analog 2,5-anhydro-D-mannitol suggesting that the enzyme is inhibited by the furanose form of fructose." @default.
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- W2740240183 date "1983-01-01" @default.
- W2740240183 modified "2023-09-27" @default.
- W2740240183 title "Purification and properties of the P-fructofuranosidase from Kluyveromyces fragilis" @default.
- W2740240183 hasPublicationYear "1983" @default.
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