Abstract
An intracellular β-fructofuranosidase (EC 3.2.1.26) from Aspergillus niger IMI 303386 was purified to homogeneity according to SDS-PAGE by (NH 4) 2SO 4 precipitation, DEAE Sepharose Fast Flow ion-exchange chromatography and Ultrogel AcA44 gelfiltration. This protocol gave 50-fold of purification and 42% recovery of enzyme activity. The molecular mass of β-fructofuranosidase from A. niger was estimated to be in the range from 120 to 130 kDa. This enzyme shows two protein species on isoelectric focusing. The p I value of major and minor protein species was calculated to be 5.4 and 4.4, respectively. Ba 2+, Mg 2+, Ca 2+ and sodium-EDTA are activators, while Hg 2+, Ag + and Ni 2+ are strong inhibitors of β-fructofuranosidase. The enzyme is completely stable in the pH range from 4 up to 8 and has a pH optimum of 5.5. The optimum temperature of β-fructofuranosidase was 50 °C and enzyme is stable up to 55 °C. More than 90% of residual activity was retained after 5 h incubation. β-Fructofuranosidase from A. niger IMI 303386 is a glycoprotein with the carbohydrate content of 17%.
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