Open AccessCovalent Immobilization of α-Galactosidase from Penicillium griseoroseum and its Application in Oligosaccharides Hydrolysis
Author(s) -
Daniel Luciano Falkoski,
Valéria Monteze Guimarães,
Marisa Vieira de Queiroz,
Elza Fernandes de Araújo,
Maíra Nicolau de Almeida,
Everaldo Gonçalves de Barros,
Sebastião Tavares de Rezende
Publication year - 2008
Publication title -
applied biochemistry and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.558
H-Index - 111
eISSN - 1559-0291
pISSN - 0273-2289
DOI - 10.1007/s12010-008-8387-9
Subject(s) - chemistry , hydrolysis , stachyose , immobilized enzyme , raffinose , glutaraldehyde , incubation , chromatography , covalent bond , penicillium , enzyme assay , enzyme , galactosidases , alpha galactosidase , incubation period , beta galactosidase , biochemistry , food science , organic chemistry , sucrose , gene , fabry disease , medicine , gene expression , disease , pathology
Partially purified alpha-Galactosidase from Penicillium griseoroseum was immobilized onto modified silica using glutaraldehyde linkages. The effective activity of immobilized enzyme was 33%. Free and immobilized alpha-galactosidase showed optimal activity at 45 degrees C and pH values of 5 and 4, respectively. Immobilized alpha-galactosidase was more stable at higher temperatures and pH values. Immobilized alpha-galactosidase from P. griseoroseum maintained 100% activity after 24 h of incubation at 40 degrees C, while free enzyme showed only 32% activity under the same incubation conditions. Defatted soybean flour was treated with free and immobilized alpha-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 alpha-galactosidase respectively. Immobilized alpha-galactosidase was reutilized eight times without any decrease in its activity.
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