Covalent immobilization of α-Galactosidase from Penicillium griseoroseum and its application in Oligosaccharides Hydrolysis
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. Imm...
| Authors: | , , , , , , |
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| Format: | article |
| Status: | Published version |
| Publication Date: | 2008 |
| Country: | Brasil |
| Institution: | Universidade Federal de Viçosa (UFV) |
| Repository: | LOCUS Repositório Institucional da UFV |
| Language: | English |
| OAI Identifier: | oai:locus.ufv.br:123456789/19134 |
| Online Access: | https://doi.org/10.1007/s12010-008-8387-9 http://www.locus.ufv.br/handle/123456789/19134 |
| Access Level: | Open access |
| Keyword: | Penicillium griseoroseum α-Galactosidase Enzyme immobilization Modified silica Raffinose oligosaccharides Soybean products |
| Summary: | 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. |
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