Production of fructooligosaccharides from sucrose by a transfructosylase from Aspergillus niger

Abstract

A strain of Aspergillus niger isolated from sugarcane fields, produced an extracellular transfructosylase in the culture medium. Sucrose and raffinose induced the production to the enzyme, which was purified by 138-fold. The optimum pH for activity and stability were 5.5 and 6.5, respectively. Its optimum temperature was 55°C. The enzyme hydrolysed sucrose rapidly and simultaneously formed fructooligosaccharides by transfructosylation.

Production of fructooligosaccharides by β‐fructofuranosidase from Aspergillus sp 27H

“…The highest values of transfructosylating activity were obtained at pH 5.5-6.0, although the enzyme maintained high activity in the pH range 5.0-6.5. These results differ from those for Aspergillus phoenicis 10 and Arthrobacter sp k-1 enzymes 11 which exhibited optimal pH values of 8.0 and 6.5-6.8, respectively, but are similar to those for β-fructofuranosidase from Aspergillus niger, 12 A japonicus 13 and Penicillium rugulosum. 14 On the other hand, the hydrolytic activity of β-fructofuranosidase from Aspergillus sp 27H was very low by comparison with its transfructosylating activity in the range of pH evaluated.…”

“…Similar results were obtained by other researchers for Aureobasidium pullulans, 15 Aspergillus japonicus 16,17 and A niger, 12 which have already been proposed as appropriate sources of enzymes for industrial use.…”

Media optimization for β-Fructofuranosidase production by Aspergillus oryzae

“…Only the sucrose-grown culture possessed high levels of mycelium and extracellular FTase activities, indicating that sucrose is the best inducer for β-fructofuranosidase biosynthesis. Similar results were found for the β-fructofuranosidase produced by Aspergillus japonicus TIT-90076 (Chen and Liu 1996) and A. niger (Park and Almeida 1991). When fructose, maltose and glucose were used, enzyme synthesis was significantly decreased, although good growth was achieved.…”

Kinetics and modeling of fructo‐oligosaccharide synthesis by immobilized fructosyltransferase from Rhodotorula sp.

“…These results are slightly different from the literature data. According to Cruz et 23 noticed a production increase of FOS when the sucrose concentration was increased from 30% to 60%, which was explained by water competition and substrate used as acceptor in the reaction catalyzed by β-frutosyltranferase.…”