Processing of soybean products by semipurified plant and microbial α-Galactosidases
Autor(a) principal: | |
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Data de Publicação: | 2006 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | https://doi.org/10.1021/jf0617162 http://www.locus.ufv.br/handle/123456789/19136 |
Resumo: | Galactooligosaccharides (GO) are responsible for intestinal disturbances following ingestion of legume-derived products. Enzymatic reduction of GO level in these products is highly desirable to improve their acceptance. For this purpose, plant and microbial semipurified α-galactosidases were used for GO hydrolysis in soybean flour and soy molasses. α-Galactosidases from soybean germinating seeds, Aspergillus terreus, and Penicillium griseoroseum presented maximal activities at pH 4.0−5.0 and 45−65 °C. The KM,app values determined for raffinose by the soybean, A. terreus, and P. griseoroseum α-galactosidases were 3.44, 19.39, and 20.67 mM, respectively. The enzymes were completely inhibited by Ag+ and Hg2+, whereas only soybean enzyme was inhibited by galactose. A. terreus α-galactosidase was more thermostable than the enzymes from the other two sources. This enzyme maintained about 100% of its original activity after 3 h at 60 °C. The microbial α-galactosidases were more efficient for reducing GO in soybean flour and soy molasses than soybean enzyme. |
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Falkoski, Daniel L.Guimarães, Valéria M.Callegari, Carina M.Reis, Angélica P.Barros, Everaldo G. deRezende, Sebastião T. de2018-04-25T17:52:32Z2018-04-25T17:52:32Z2006-05-1215205118https://doi.org/10.1021/jf0617162http://www.locus.ufv.br/handle/123456789/19136Galactooligosaccharides (GO) are responsible for intestinal disturbances following ingestion of legume-derived products. Enzymatic reduction of GO level in these products is highly desirable to improve their acceptance. For this purpose, plant and microbial semipurified α-galactosidases were used for GO hydrolysis in soybean flour and soy molasses. α-Galactosidases from soybean germinating seeds, Aspergillus terreus, and Penicillium griseoroseum presented maximal activities at pH 4.0−5.0 and 45−65 °C. The KM,app values determined for raffinose by the soybean, A. terreus, and P. griseoroseum α-galactosidases were 3.44, 19.39, and 20.67 mM, respectively. The enzymes were completely inhibited by Ag+ and Hg2+, whereas only soybean enzyme was inhibited by galactose. A. terreus α-galactosidase was more thermostable than the enzymes from the other two sources. This enzyme maintained about 100% of its original activity after 3 h at 60 °C. The microbial α-galactosidases were more efficient for reducing GO in soybean flour and soy molasses than soybean enzyme.engJournal of Agricultural and Food Chemistryv. 54, n. 26, p. 10184–10190, December 2006American Chemical Societyinfo:eu-repo/semantics/openAccessSoybeanα-galactosidaseGalactooligosaccharidesAspergillusPenicilliumProcessing of soybean products by semipurified plant and microbial α-Galactosidasesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdfTexto completoapplication/pdf98552https://locus.ufv.br//bitstream/123456789/19136/1/artigo.pdfdb64807c9e9ed6f7084414c8aab76ba3MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/19136/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILartigo.pdf.jpgartigo.pdf.jpgIM Thumbnailimage/jpeg5142https://locus.ufv.br//bitstream/123456789/19136/3/artigo.pdf.jpg93e7851ce29d239c783dbc456197ffdfMD53123456789/191362018-04-25 23:00:37.771oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-04-26T02:00:37LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
Processing of soybean products by semipurified plant and microbial α-Galactosidases |
title |
Processing of soybean products by semipurified plant and microbial α-Galactosidases |
spellingShingle |
Processing of soybean products by semipurified plant and microbial α-Galactosidases Falkoski, Daniel L. Soybean α-galactosidase Galactooligosaccharides Aspergillus Penicillium |
title_short |
Processing of soybean products by semipurified plant and microbial α-Galactosidases |
title_full |
Processing of soybean products by semipurified plant and microbial α-Galactosidases |
title_fullStr |
Processing of soybean products by semipurified plant and microbial α-Galactosidases |
title_full_unstemmed |
Processing of soybean products by semipurified plant and microbial α-Galactosidases |
title_sort |
Processing of soybean products by semipurified plant and microbial α-Galactosidases |
author |
Falkoski, Daniel L. |
author_facet |
Falkoski, Daniel L. Guimarães, Valéria M. Callegari, Carina M. Reis, Angélica P. Barros, Everaldo G. de Rezende, Sebastião T. de |
author_role |
author |
author2 |
Guimarães, Valéria M. Callegari, Carina M. Reis, Angélica P. Barros, Everaldo G. de Rezende, Sebastião T. de |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Falkoski, Daniel L. Guimarães, Valéria M. Callegari, Carina M. Reis, Angélica P. Barros, Everaldo G. de Rezende, Sebastião T. de |
dc.subject.pt-BR.fl_str_mv |
Soybean α-galactosidase Galactooligosaccharides Aspergillus Penicillium |
topic |
Soybean α-galactosidase Galactooligosaccharides Aspergillus Penicillium |
description |
Galactooligosaccharides (GO) are responsible for intestinal disturbances following ingestion of legume-derived products. Enzymatic reduction of GO level in these products is highly desirable to improve their acceptance. For this purpose, plant and microbial semipurified α-galactosidases were used for GO hydrolysis in soybean flour and soy molasses. α-Galactosidases from soybean germinating seeds, Aspergillus terreus, and Penicillium griseoroseum presented maximal activities at pH 4.0−5.0 and 45−65 °C. The KM,app values determined for raffinose by the soybean, A. terreus, and P. griseoroseum α-galactosidases were 3.44, 19.39, and 20.67 mM, respectively. The enzymes were completely inhibited by Ag+ and Hg2+, whereas only soybean enzyme was inhibited by galactose. A. terreus α-galactosidase was more thermostable than the enzymes from the other two sources. This enzyme maintained about 100% of its original activity after 3 h at 60 °C. The microbial α-galactosidases were more efficient for reducing GO in soybean flour and soy molasses than soybean enzyme. |
publishDate |
2006 |
dc.date.issued.fl_str_mv |
2006-05-12 |
dc.date.accessioned.fl_str_mv |
2018-04-25T17:52:32Z |
dc.date.available.fl_str_mv |
2018-04-25T17:52:32Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://doi.org/10.1021/jf0617162 http://www.locus.ufv.br/handle/123456789/19136 |
dc.identifier.issn.none.fl_str_mv |
15205118 |
identifier_str_mv |
15205118 |
url |
https://doi.org/10.1021/jf0617162 http://www.locus.ufv.br/handle/123456789/19136 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
v. 54, n. 26, p. 10184–10190, December 2006 |
dc.rights.driver.fl_str_mv |
American Chemical Society info:eu-repo/semantics/openAccess |
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American Chemical Society |
eu_rights_str_mv |
openAccess |
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application/pdf |
dc.publisher.none.fl_str_mv |
Journal of Agricultural and Food Chemistry |
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Journal of Agricultural and Food Chemistry |
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