Artigo
Covalent immobilization of α-Galactosidase from Penicillium griseoroseum and its application in Oligosaccharides Hydrolysis
Autor
Falkoski, Daniel Luciano
Guimarães, Valéria Monteze
Queiroz, Marisa Vieira de
Araújo, Elza Fernandes de
Almeida, Maíra Nicolau de
Barros, Everaldo Gonçalves de
Rezende, Sebastião Tavares de
Institución
Resumen
Partially purified α-Galactosidase from Penicillium griseoroseum was immobilized onto modified silica using glutaraldehyde linkages. The effective activity of immobilized enzyme was 33%. Free and immobilized α-galactosidase showed optimal activity at 45 °C and pH values of 5 and 4, respectively. Immobilized α-galactosidase was more stable at higher temperatures and pH values. Immobilized α-galactosidase from P. griseoroseum maintained 100% activity after 24 h of incubation at 40 °C, while free enzyme showed only 32% activity under the same incubation conditions. Defatted soybean flour was treated with free and immobilized α-galactosidase in batch reactors. After 8 h of incubation, stachyose was completely hydrolyzed in both treatments. After 8 h of incubation, 39% and 70% of raffinose was hydrolyzed with free and immobilized α-galactosidase respectively. Immobilized α-galactosidase was reutilized eight times without any decrease in its activity.