Abstract

Within this study, the investigation of potential selective immobilization of fructosyltransferase (FTase) derived from Aspergillus aculeatus (from commercial enzyme preparation Pectinex® Ultra SP-L) onto the polystyrenic macroporous resin Purolite® A109 and its further utilization for the synthesis of a highly valuable group of prebiotic compounds named fructo-oligosaccharides (FOS), was performed. The obtained results suggest that partial purification of fructosyltransferase from complex enzyme mixture with predominant pectinase activity (ratio of activity immobilization yields around 20.0) occurred by performing a simple immobilization protocol, provided that immobilization lasted for 5 h using an enzyme concentration of 50 mg g−1 of support under slightly acidic conditions (pH 6.0). Immobilized preparation was thereafter successfully utilized for FOS synthesis (56–59 % FOS of total sugars) in both a batch and air-lift reactor system. Operational stability study proved the exceptionally high potential of immobilized preparation for reproducible and cost-effective application, since 90 % of initial activity was preserved after ten consecutive reaction cycles. Thereafter, a prospectus for continuous production of FOS in the air-lift reactor was assayed. Achieved yields, 53 % FOS of total sugars for at least 9 h, indicated the great suitability of the obtained immobilized preparation for application in large-scale systems.

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