Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides

Detalhes bibliográficos
Autor(a) principal: Ferreira, Joana Gasperazzo
Data de Publicação: 2011
Outros Autores: Reis, Angélica Pataro, Guimarães, Valéria Monteze, Falkoski, Daniel Luciano, Silva Fialho, Lílian da, 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/s12010-011-9198-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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spelling 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
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