PROPERTIES AND APPLICATION OF B-FRUCTOFURANOSIDASE FROM ASPERGILLUS JAPONICUS 3.3556

In this study, beta-fructofuranosidase from Aspergillus japonicus was purified to homogeneity according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis by (NH(4))(2)SO(4) precipitation and gel filtration on sephadex G-100. The molecular mass of FFase from Aspergillus japonicus 3.3556 was estimated to be 89 kDa. Parameters like temperature, pH, and metal ions had different effects on FFase activity. The result showed that Fe(3+) and Mg(2+) were the inhibitors of FFase. The enzyme was completely stable in the pH range from 5 to 7 with the optimum pH of 5.5. The enzyme was stable in the temperature range from 40 to 60C with the optimum temperature of 50C. The K(m) and V(max) values for FFase were determined to be 59.88 mmol/L and 0.9421 mu mol/mL/min, respectively. FFase activity increased with the increase of sucrose concentration. FFase could produce 1-kestose and nystose from sucrose by fructosyl-transferring activity.