Covalent immobilization of α-Galactosidase from Penicillium griseoroseum and its application in Oligosaccharides Hydrolysis

• Autor(a) principal: Falkoski, Daniel Luciano
• Data de Publicação: 2008
• Outros Autores: Guimarães, Valéria Monteze, Queiroz, Marisa Vieira de, Araújo, Elza Fernandes de, Almeida, Maíra Nicolau de, Barros, Everaldo Gonçalves de, Rezende, Sebastião Tavares de
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: LOCUS Repositório Institucional da UFV
• Texto Completo: https://doi.org/10.1007/s12010-008-8387-9; http://www.locus.ufv.br/handle/123456789/19134
• topic: Penicillium griseoroseum; α-Galactosidase; Enzyme immobilization; Modified silica; Raffinose oligosaccharides; Soybean products

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.