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https://locus.ufv.br//handle/123456789/18612
Tipo: | Artigo |
Título: | Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides |
Autor(es): | Ferreira, Joana Gasperazzo Reis, Angélica Pataro Guimarães, Valéria Monteze Falkoski, Daniel Luciano Silva Fialho, Lílian da Rezende, Sebastião Tavares de |
Abstract: | α-Galactosidases has the potential to hydrolyze α-1-6 linkages in raffinose family oligosaccharides (RFO). Aspergillus terreus cells cultivated on wheat bran produced three extracellular forms of α-galactosidases (E1, E2, and E3). E1 and E2 α-galactosidases presented maximal activities at pH 5, while E3 α-galactosidase was more active at pH 5.5. The E1 and E2 enzymes showed stability for 6 h at pH 4–7. Maximal activities were determined at 60, 55, and 50°C, for E1, E2, and E3 α-galactosidase, respectively. E2 α-galactosidase retained 90% of its initial activity after 70 h at 50°C. The enzymes hydrolyzed ρNPGal, melibiose, raffinose and stachyose, and E1 and E2 enzymes were able to hydrolyze guar gum and locust bean gum substrates. E1 and E3 α-galactosidases were completely inhibited by Hg2+, Ag+, and Cu2+. The treatment of RFO present in soy milk with the enzymes showed that E1 α-galactosidase reduced the stachyose content to zero after 12 h of reaction, while E2 promoted total hydrolysis of raffinose. The complete removal of the oligosaccharides in soy milk could be reached by synergistic action of both enzymes |
Palavras-chave: | α-Galactosidase Aspergillus terreus Raffinose Stachyose Soybean Anti-nutritional factors |
Editor: | Applied Biochemistry and Biotechnology |
Tipo de Acesso: | Springer Science+Business Media, LLC |
URI: | https://doi.org/10.1007/s12010-011-9198-y http://www.locus.ufv.br/handle/123456789/18612 |
Data do documento: | 18-Fev-2011 |
Aparece nas coleções: | Artigos |
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artigo.pdf Until 2100-05-28 | Texto completo | 249,58 kB | Adobe PDF | Visualizar/Abrir ACESSO RESTRITO |
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