Fructooligosaccharides synthesis by highly stable immobilized β-fructofuranosidase from Aspergillus aculeatus

Abstract

The enzymatic synthesis of fructooligosaccharides (FOS) was carried out using a partially purified β-fructofuranosidase from the commercial enzyme preparation Viscozyme L. Partial purification of β-fructofuranosidase from Viscozyme L was done by batch adsorption using ion-exchange resin DEAE-Sepharose, showing a 6-fold increase in specific activity. The biocatalyst was then covalently immobilized on glutaraldehyde-activated chitosan particles. Thermal stability of the biocatalyst was evaluated at 50 °C and 60 °C, being around 100 times higher at 60 °C when compared to the free enzyme. The immobilized biocatalyst was reused 50 times for FOS production (100 min per batch at 50 °C and pH 5.5) without significant loss of activity. The average yield (grams of FOS per grams of initial sucrose) was 55%. The immobilization process combined with partial purification method resulted in a derivative with activity of 1230 Ut/g, which is among the best for FOS production.

Immobilization of Fusarium graminearum β-d-fructofuranosidase using alternative cellulosic supports: Stabilization and production of fructooligosaccharides

“…Microbial fructofuranosidases have been immobilized on traditional supports, including calcium alginate (13), alginate-silica matrix (14), and nylon (15), as well as on new materials such as nanoparticles (16). Fungal fructofuranosidases have been also immobilized on different cellulosic supports such as wheat straw, corncobs, coffee husks, cork oak, loofa sponge (4), as well as glutaraldehydeactivated chitosan (17), and WA-30 anion-exchange resin (18). Despite the use of the above-mentioned cellulosic supports to immobilize fructofuranosidase, the discovery of new cellulosic materials that can reduce the costs associated with enzymatic hydrolysis and consequently lower the cost of the end product would increase industrial usage.…”

Comparison of immobilized and free enzyme systems in industrial production of short‐chain fructooligosaccharides from sucrose using a techno‐economic approach

“…Another possible shortcoming is that, unlike most conventional heterogenous catalysts, the immobilized biocatalyst in many cases experiences a substantial loss in activity after a limited number of reuses, typically between 7 and 15 cycles of reuse . As a result of the technical and functional advantages of the immobilized over the free enzyme reported in literature, many authors have proposed that the industrial application of an immobilized β ‐fructofuranosidase in scFOS production may offer economic advantages over the free enzyme …”

Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase with transfructosylating activity

“…Commercial preparations of enzymes from strains of Aspergillus aculeatus (Pectinex Ultra SP‐L and Viscozyme L) and Aspergillus niger (Rohapect CM), with high transfructosylating activity have been successfully used to synthesize FOS. Moreover, studies involving the production of FFases were already reported using Aspergillus japonicus , A. niger and other filamentous fungi, such as Penicillium oxalicum , Penicillium citreonigrum , Penicillium sizovae , and Cladosporium cladosporioides , the last two standing out in the production of neo‐FOS and the last one in that of FOS using seawater .…”