Fructo-oligosaccharides production by an Aspergillus aculeatus commercial enzyme preparation with fructosyltransferase activity covalently immobilized on Fe 3 O 4 -chitosan-magnetic nanoparticles

• Published in: International journal of biological macromolecules Vol. 150; p. 922
• Main Authors: de Oliveira, Rodrigo Lira, da Silva, Marcos Fellipe, da Silva, Suzana Pedroza, de Araújo, Ana Cláudia Vaz, Cavalcanti, Jorge Vinícius Fernandes Lima, Converti, Attilio, Porto, Tatiana Souza
• Format: Journal Article
• Language: English
• Published: Netherlands 01-05-2020
• Subjects: Aspergillus - enzymology; Chitosan - chemistry; Enzyme Activation; Enzyme Stability; Enzymes, Immobilized - chemistry; Enzymes, Immobilized - metabolism; Glutaral; Hexosyltransferases - chemistry; Hexosyltransferases - metabolism; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Magnetite Nanoparticles - chemistry; Oligosaccharides - biosynthesis; Temperature; Trisaccharides; Magnetic nanoparticles; Fructosyltransferase; Fructo-oligosaccharides
• ISSN: 1879-0003

Pectinex Ultra SP-L, a commercial enzyme preparation with fructosyltransferase activity, was successfully immobilized by covalent binding to Fe
O
-chitosan- magnetic nanoparticles. Immobilization carried out according to a 2
-full factorial design where glutaraldehyde concentration, activation time and time of contact between enzyme and support were selected as the independent variables and immobilization yield as the response. The highest immobilization yield (94.84%) was obtained using 3.0% (v/v) glutaraldehyde and activation and contact times of 180 and 30 min, respectively. The immobilized biocatalyst, which showed for both hydrolytic and transfructosylating activities optimum pH and temperature of 7.0 and 60 °C, respectively, retained 70 and 86% of them after 6 cycles of reuse. A kinetic/thermodynamic study focused on thermal inactivation of the immobilized construct indicated high thermostability at temperatures commonly used for fructo-oligosaccharides (FOS) production. Maximum FOS concentration obtained in lab-scale experiments was 101.56 g L
, with predominant presence of 1-kestose in the reaction mixture. The results obtained in this study suggest that the immobilized-enzyme preparation may be effectively exploited for FOS production and easily recovered from the reaction mixture by action of a magnetic field.