Selective synthesis of galactooligosaccharides containing β(1→3) linkages with Beta-galactosidase from Bifidobacterium bifidum

The transglycosylation activity of a novel commercial β-galactosidase from Bifidobacterium bifidum (Saphera) was evaluated. The optimal conditions of operation of this enzyme, measured with o-nitrophenyl-β-D-galactopyranoside, were 40 °C and pH around 6.0. Although at low lactose concentrations the...

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Autores: Füreder, Vera, Rodríguez Colinas, Bárbara, Cervantes, Fadia V., Fernández-Arrojo, Lucía, Poveda, Ana, Jiménez-Barbero, Jesús, Ballesteros, Antonio O., Plou, Francisco J.
Tipo de recurso: artículo
Fecha de publicación:2020
País:España
Institución:Universidad Francisco de Vitoria
Repositorio:DDFV. Repositorio Institucional de la Universidad Francisco de Vitoria
Idioma:inglés
OAI Identifier:oai:ddfv.ufv.es:10641/2623
Acceso en línea:http://hdl.handle.net/10641/2623
Access Level:acceso abierto
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spelling Selective synthesis of galactooligosaccharides containing β(1→3) linkages with Beta-galactosidase from Bifidobacterium bifidumFüreder, VeraRodríguez Colinas, BárbaraCervantes, Fadia V.Fernández-Arrojo, LucíaPoveda, AnaJiménez-Barbero, JesúsBallesteros, Antonio O.Plou, Francisco J.The transglycosylation activity of a novel commercial β-galactosidase from Bifidobacterium bifidum (Saphera) was evaluated. The optimal conditions of operation of this enzyme, measured with o-nitrophenyl-β-D-galactopyranoside, were 40 °C and pH around 6.0. Although at low lactose concentrations the character of this enzyme was basically hydrolytic, an increase of lactose concentration to 400 g/L resulted in a significant formation (107.2 g/L, 27% yield) of prebiotic galactooligosaccharides (GOS). The maximum amount of GOS was obtained at a lactose conversion of approximately 90%, which contrasts with other β-galactosidases, for which the highest GOS yield is achieved at 40-50% lactose conversion. Using HPAEC-PAD, semipreparative HPLC-HILIC, MS, 1D and 2D NMR, we determined the structure of most of the GOS synthesized by this enzyme. The main identified products were Gal-β(13)-Gal-β(14)-Glc (3´-O-Beta-galactosyllactose), Gal-β(1→6)-Glc (allolactose), Gal-β(13)-Glc (3-galactosyl-glucose), Galβ(1→3)-Gal (3-galactobiose) and the tetrasaccharide Gal-β(13)-Gal-β(13)-Galβ(14)-Glc. In general, the B. bifidum β-galactosidase showed a tendency to form β(13) linkages followed by β(16), and more scarcely β(14).20202020-01-0120202020-01-01journal articlehttp://purl.org/coar/resource_type/c_6501SMURhttp://purl.org/coar/version/c_71e4c1898caa6e32info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10641/2623reponame:DDFV. Repositorio Institucional de la Universidad Francisco de Vitoriainstname:Universidad Francisco de VitoriaInglésengopen accesshttp://purl.org/coar/access_right/c_abf2Atribución-NoComercial-SinDerivadas 3.0 Españahttp://creativecommons.org/licenses/by-nc-nd/3.0/es/info:eu-repo/semantics/openAccessoai:ddfv.ufv.es:10641/26232026-06-11T12:44:57Z
dc.title.none.fl_str_mv Selective synthesis of galactooligosaccharides containing β(1→3) linkages with Beta-galactosidase from Bifidobacterium bifidum
title Selective synthesis of galactooligosaccharides containing β(1→3) linkages with Beta-galactosidase from Bifidobacterium bifidum
spellingShingle Selective synthesis of galactooligosaccharides containing β(1→3) linkages with Beta-galactosidase from Bifidobacterium bifidum
Füreder, Vera
title_short Selective synthesis of galactooligosaccharides containing β(1→3) linkages with Beta-galactosidase from Bifidobacterium bifidum
title_full Selective synthesis of galactooligosaccharides containing β(1→3) linkages with Beta-galactosidase from Bifidobacterium bifidum
title_fullStr Selective synthesis of galactooligosaccharides containing β(1→3) linkages with Beta-galactosidase from Bifidobacterium bifidum
title_full_unstemmed Selective synthesis of galactooligosaccharides containing β(1→3) linkages with Beta-galactosidase from Bifidobacterium bifidum
title_sort Selective synthesis of galactooligosaccharides containing β(1→3) linkages with Beta-galactosidase from Bifidobacterium bifidum
dc.creator.none.fl_str_mv Füreder, Vera
Rodríguez Colinas, Bárbara
Cervantes, Fadia V.
Fernández-Arrojo, Lucía
Poveda, Ana
Jiménez-Barbero, Jesús
Ballesteros, Antonio O.
Plou, Francisco J.
author Füreder, Vera
author_facet Füreder, Vera
Rodríguez Colinas, Bárbara
Cervantes, Fadia V.
Fernández-Arrojo, Lucía
Poveda, Ana
Jiménez-Barbero, Jesús
Ballesteros, Antonio O.
Plou, Francisco J.
author_role author
author2 Rodríguez Colinas, Bárbara
Cervantes, Fadia V.
Fernández-Arrojo, Lucía
Poveda, Ana
Jiménez-Barbero, Jesús
Ballesteros, Antonio O.
Plou, Francisco J.
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv
description The transglycosylation activity of a novel commercial β-galactosidase from Bifidobacterium bifidum (Saphera) was evaluated. The optimal conditions of operation of this enzyme, measured with o-nitrophenyl-β-D-galactopyranoside, were 40 °C and pH around 6.0. Although at low lactose concentrations the character of this enzyme was basically hydrolytic, an increase of lactose concentration to 400 g/L resulted in a significant formation (107.2 g/L, 27% yield) of prebiotic galactooligosaccharides (GOS). The maximum amount of GOS was obtained at a lactose conversion of approximately 90%, which contrasts with other β-galactosidases, for which the highest GOS yield is achieved at 40-50% lactose conversion. Using HPAEC-PAD, semipreparative HPLC-HILIC, MS, 1D and 2D NMR, we determined the structure of most of the GOS synthesized by this enzyme. The main identified products were Gal-β(13)-Gal-β(14)-Glc (3´-O-Beta-galactosyllactose), Gal-β(1→6)-Glc (allolactose), Gal-β(13)-Glc (3-galactosyl-glucose), Galβ(1→3)-Gal (3-galactobiose) and the tetrasaccharide Gal-β(13)-Gal-β(13)-Galβ(14)-Glc. In general, the B. bifidum β-galactosidase showed a tendency to form β(13) linkages followed by β(16), and more scarcely β(14).
publishDate 2020
dc.date.none.fl_str_mv 2020
2020-01-01
2020
2020-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
SMUR
http://purl.org/coar/version/c_71e4c1898caa6e32
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10641/2623
url http://hdl.handle.net/10641/2623
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución-NoComercial-SinDerivadas 3.0 España
http://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución-NoComercial-SinDerivadas 3.0 España
http://creativecommons.org/licenses/by-nc-nd/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:DDFV. Repositorio Institucional de la Universidad Francisco de Vitoria
instname:Universidad Francisco de Vitoria
instname_str Universidad Francisco de Vitoria
reponame_str DDFV. Repositorio Institucional de la Universidad Francisco de Vitoria
collection DDFV. Repositorio Institucional de la Universidad Francisco de Vitoria
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300724

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