Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | https://doi.org/10.1007/s12010-011-9198-y http://www.locus.ufv.br/handle/123456789/18612 |
Resumo: | 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 |
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Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharidesα-GalactosidaseAspergillus terreusRaffinoseStachyoseSoybeanAnti-nutritional factorsα-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 enzymesApplied Biochemistry and Biotechnology2018-04-04T10:02:13Z2018-04-04T10:02:13Z2011-02-18info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlepdfapplication/pdf15590291https://doi.org/10.1007/s12010-011-9198-yhttp://www.locus.ufv.br/handle/123456789/18612engv. 164, Issue 7, p. 1111–1125, August 2011Springer Science+Business Media, LLCinfo:eu-repo/semantics/openAccessFerreira, Joana GasperazzoReis, Angélica PataroGuimarães, Valéria MontezeFalkoski, Daniel LucianoSilva Fialho, Lílian daRezende, Sebastião Tavares dereponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFV2024-07-12T07:09:48Zoai:locus.ufv.br:123456789/18612Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452024-07-12T07:09:48LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.none.fl_str_mv |
Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides |
title |
Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides |
spellingShingle |
Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides Ferreira, Joana Gasperazzo α-Galactosidase Aspergillus terreus Raffinose Stachyose Soybean Anti-nutritional factors |
title_short |
Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides |
title_full |
Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides |
title_fullStr |
Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides |
title_full_unstemmed |
Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides |
title_sort |
Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides |
author |
Ferreira, Joana Gasperazzo |
author_facet |
Ferreira, Joana Gasperazzo Reis, Angélica Pataro Guimarães, Valéria Monteze Falkoski, Daniel Luciano Silva Fialho, Lílian da Rezende, Sebastião Tavares de |
author_role |
author |
author2 |
Reis, Angélica Pataro Guimarães, Valéria Monteze Falkoski, Daniel Luciano Silva Fialho, Lílian da Rezende, Sebastião Tavares de |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Ferreira, Joana Gasperazzo Reis, Angélica Pataro Guimarães, Valéria Monteze Falkoski, Daniel Luciano Silva Fialho, Lílian da Rezende, Sebastião Tavares de |
dc.subject.por.fl_str_mv |
α-Galactosidase Aspergillus terreus Raffinose Stachyose Soybean Anti-nutritional factors |
topic |
α-Galactosidase Aspergillus terreus Raffinose Stachyose Soybean Anti-nutritional factors |
description |
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 |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-02-18 2018-04-04T10:02:13Z 2018-04-04T10:02:13Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
15590291 https://doi.org/10.1007/s12010-011-9198-y http://www.locus.ufv.br/handle/123456789/18612 |
identifier_str_mv |
15590291 |
url |
https://doi.org/10.1007/s12010-011-9198-y http://www.locus.ufv.br/handle/123456789/18612 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
v. 164, Issue 7, p. 1111–1125, August 2011 |
dc.rights.driver.fl_str_mv |
Springer Science+Business Media, LLC info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Springer Science+Business Media, LLC |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
pdf application/pdf |
dc.publisher.none.fl_str_mv |
Applied Biochemistry and Biotechnology |
publisher.none.fl_str_mv |
Applied Biochemistry and Biotechnology |
dc.source.none.fl_str_mv |
reponame:LOCUS Repositório Institucional da UFV instname:Universidade Federal de Viçosa (UFV) instacron:UFV |
instname_str |
Universidade Federal de Viçosa (UFV) |
instacron_str |
UFV |
institution |
UFV |
reponame_str |
LOCUS Repositório Institucional da UFV |
collection |
LOCUS Repositório Institucional da UFV |
repository.name.fl_str_mv |
LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV) |
repository.mail.fl_str_mv |
fabiojreis@ufv.br |
_version_ |
1817559903989923840 |