Abstract:
Fructooligosaccharides (FOS) are sweeteners produced through the use of enzymes called fructosyltransferases (FTases) (EC 2.4.1.9). However, FTase reuse is meagre and the cost of the enzyme production is high, making FOS production economically unfeasible. In order to address these issues, this study aims to immobilize cells from Aspergillus oryzae IPT-301, containing FTase enzyme previously glutaraldehyde-crosslinked, by means of entrapment in calcium alginate beads. The conditions to obtain the particles, such as alginate type, mycelium mechanical dispersion, degree of crosslinking, size of the beads, and their reflections on transfructosylation activity (AT) were evaluated previously. The highest AT used low-viscosity alginate solution (4.0% w/w) crosslinked with calcium chloride (0.2 mol L−1) and beads of mean diameter 2.15 mm. The entrapment conditions were complemented by conducting the reaction under different temperatures, pH values, substrate concentrations and by reusing the beads. The highest transfructosylation activities were obtained under reaction conditions of 50 °C, pH 5.5 and substrate concentration 400 g L−1. The AT levels found with the glutaraldehyde-crosslinked and entrapped cells in calcium alginate were ≈70% higher than the ones obtained with free cells, not glutaraldehyde-crosslinked. Moreover, the immobilized cells (crosslinked +entrapped) retained their AT up to the third cycle of total sucrose depletion in the reaction medium, attesting to the potential use of the beads in continuous FOS production.
Reference:
GONÇALVES, Maria Carolina P.; MORALES, Sergio A.V.; SILVA, Elda Sabino da; MAIORANO, Alfredo Eduardo, PERNA, Rafael; KIECKBUSCH, Theo G. Entrapment of glutaraldehyde-crosslinked cells from Aspergillus oryzae IPT -301 in calcium alginate for high transfructosylation activity. Journal Chemical Technologyand Biotechnology, v.95, n.10, p.2463-2472, Sept., 2020.
Access to the article on the Journal’s website:
https://onlinelibrary.wiley.com/doi/abs/10.1002/jctb.6429
Fructooligosaccharides (FOS) are sweeteners produced through the use of enzymes called fructosyltransferases (FTases) (EC 2.4.1.9). However, FTase reuse is meagre and the cost of the enzyme production is high, making FOS production economically unfeasible. In order to address these issues, this study aims to immobilize cells from Aspergillus oryzae IPT-301, containing FTase enzyme previously glutaraldehyde-crosslinked, by means of entrapment in calcium alginate beads. The conditions to obtain the particles, such as alginate type, mycelium mechanical dispersion, degree of crosslinking, size of the beads, and their reflections on transfructosylation activity (AT) were evaluated previously. The highest AT used low-viscosity alginate solution (4.0% w/w) crosslinked with calcium chloride (0.2 mol L−1) and beads of mean diameter 2.15 mm. The entrapment conditions were complemented by conducting the reaction under different temperatures, pH values, substrate concentrations and by reusing the beads. The highest transfructosylation activities were obtained under reaction conditions of 50 °C, pH 5.5 and substrate concentration 400 g L−1. The AT levels found with the glutaraldehyde-crosslinked and entrapped cells in calcium alginate were ≈70% higher than the ones obtained with free cells, not glutaraldehyde-crosslinked. Moreover, the immobilized cells (crosslinked +entrapped) retained their AT up to the third cycle of total sucrose depletion in the reaction medium, attesting to the potential use of the beads in continuous FOS production.
Reference:
GONÇALVES, Maria Carolina P.; MORALES, Sergio A.V.; SILVA, Elda Sabino da; MAIORANO, Alfredo Eduardo, PERNA, Rafael; KIECKBUSCH, Theo G. Entrapment of glutaraldehyde-crosslinked cells from Aspergillus oryzae IPT -301 in calcium alginate for high transfructosylation activity. Journal Chemical Technologyand Biotechnology, v.95, n.10, p.2463-2472, Sept., 2020.
Access to the article on the Journal’s website:
https://onlinelibrary.wiley.com/doi/abs/10.1002/jctb.6429
