Purification and Characterization ofβ-Fructofuranosidase fromAspergillus japonicusTIT-KJ1

Abstract

A beta-fructofuranosidase (EC 3.2.1.26) was purified to homogeneity from Aspergillus japonicus TIT-KJ1. The enzyme had an optimum pH for activity of 5.4 and pH stability at 7.0-8.4. The optimum temperature at pH 5.4 was 60 degrees C. The enzyme had a molecular weight of 236,000 with two subunits and an isoelectric point of pH 4.0. The enzyme was inactivated by 5 mM Hg2+ and Ag+. The enzyme had a high transfructosylating activity. Treatment of 50% (w/v) sucrose with the enzyme under optimum conditions afforded more than 55% fructooligosaccharides.

Immobilization of ?-fructofuranosidase from Aspergillus japonicus on chitosan using tris(hydroxymethyl)phosphine or glutaraldehyde as a coupling agent

“…The pH activity curve agrees with the results of Duan et al (1993) as shown in Figure 1. There were some differences in activity of the enzymes at pH 8.5 where both the immobilized enzymes were more active than the free enzyme ( Figure 1).…”

“…After cultivation, the mycelium was harvested by filtration through a 250 mesh screen. The crude Ffase (b-fructofuranosidase) was extracted from the mycelium and was partially purified by preparative isoelectric focusing electrophoresis (IEF, Bio-Rad) following the procedures suggested by Duan et al (1993).…”

“…They stimulate the growth of the beneficial Bifidobacterium in animal intestines; hence, they are used in the health foods (L'homme et al 2003). The commercial production of FOS can be developed through the enzymatic fructosyl transfer from sucrose (GF) to an acceptor that can be sucrose, 1-kestose, or nystose (Duan et al 1993). b-Fructofuranosidase (Ffase) occurs in various fungi including Aspergillus (Hidaka et al 1988, Hayashi et al 1992 and Aureobasidium species (Jung et al 1987).…”

Characterization of a thermo-tolerant mycelial β-fructofuranosidase from Aspergillus phoenicis under submerged fermentation using wheat bran as carbon source

“…As previously reported for the extracellular enzyme from A. phoenicis (Rustiguel et al, 2010), we found that 10 mM Ag þ increased the mycelial enzyme activity by 91%. Ag þ was reported to inhibit β-D-fructofuranosidase activity in A. japonicus (Duan et al, 1993) and F. oxysporum (Nishizawa et al, 1980). Metal ions can change the overall charge of proteins, thereby affecting their properties.…”

Optimization of Medium Composition and Cultivation Parameters for Fructosyltransferase Production by Penicillium aurantiogriseum AUMC 5605

“…Determination of FTase activity. Fructosyltransferase activity in culture filtrate was measured by estimating the liberated reducing sugar released from sucrose as described by Duan et al (1993) using glucose as a standard. The assay mixture contained appropriately 0.1 mL of the enzyme solution, (0.15 M Mcllvaine buffer pH 5.5) and 0.4 mL of 50% (W/V) sucrose solution.…”