Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane

Autores
Regenhardt, Silvina Andrea; Mammarella, Enrique José; Rubiolo, Amelia Catalina
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this study, ß-galactosidase enzyme from Kluyveromyces fragilis was immobilised on a commercial polyethersulfone membrane surface, 10 kDa cut-off. An integrated process, concerning the simultaneous hydrolysis–ultrafiltration of whey lactose was studied and working conditions have been fixed at 55°C and pH 6.9, the same conditions that are used for the industrial process of protein concentration. For the immobilisation, best results were obtained using 5% (v/v) of glutaraldehyde solution and 0.03 M galactose; the total activity recovery coefficient (TARC) was 44.2%. The amount of immobilised enzyme was 12.49 mg with a total activity of 86.3 LAU at 37°C, using 5% (w/v) lactose solution in phosphate buffer (100 mM pH 6.9). The stability of the immobilised enzyme was approximately 585 fold higher in comparison with the stability of free enzyme. Multipoint covalent immobilisation improves the stability of the enzyme, thereby enhancing the decision to use the membrane as a filtering element and support for the enzyme immobilisation.
Fil: Regenhardt, Silvina Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico Para la Industria Química (i); Argentina
Fil: Mammarella, Enrique José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico Para la Industria Química (i); Argentina
Fil: Rubiolo, Amelia Catalina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico Para la Industria Química (i); Argentina
Materia
LACTOSE
ENZYMATIC HYDROLYSIS
MEMBRANE BIOREACTOR
WHEY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/8866
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/8866
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membraneRegenhardt, Silvina AndreaMammarella, Enrique JoséRubiolo, Amelia CatalinaLACTOSEENZYMATIC HYDROLYSISMEMBRANE BIOREACTORWHEYhttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2In this study, ß-galactosidase enzyme from Kluyveromyces fragilis was immobilised on a commercial polyethersulfone membrane surface, 10 kDa cut-off. An integrated process, concerning the simultaneous hydrolysis–ultrafiltration of whey lactose was studied and working conditions have been fixed at 55°C and pH 6.9, the same conditions that are used for the industrial process of protein concentration. For the immobilisation, best results were obtained using 5% (v/v) of glutaraldehyde solution and 0.03 M galactose; the total activity recovery coefficient (TARC) was 44.2%. The amount of immobilised enzyme was 12.49 mg with a total activity of 86.3 LAU at 37°C, using 5% (w/v) lactose solution in phosphate buffer (100 mM pH 6.9). The stability of the immobilised enzyme was approximately 585 fold higher in comparison with the stability of free enzyme. Multipoint covalent immobilisation improves the stability of the enzyme, thereby enhancing the decision to use the membrane as a filtering element and support for the enzyme immobilisation.Fil: Regenhardt, Silvina Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico Para la Industria Química (i); ArgentinaFil: Mammarella, Enrique José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico Para la Industria Química (i); ArgentinaFil: Rubiolo, Amelia Catalina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico Para la Industria Química (i); ArgentinaVersita2013-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/8866Regenhardt, Silvina Andrea; Mammarella, Enrique José; Rubiolo, Amelia Catalina; Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane; Versita; Chemical And Process Engineering-inzynieria Chemiczna I Procesowa; 34; 3; 10-2013; 375-3852300-1925enginfo:eu-repo/semantics/altIdentifier/doi/10.2478/cpe-2013-0030info:eu-repo/semantics/altIdentifier/url/https://www.degruyter.com/view/j/cpe.2013.34.issue-3/cpe-2013-0030/cpe-2013-0030.xmlinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:30:06Zoai:ri.conicet.gov.ar:11336/8866instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:30:06.544CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane
title Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane
spellingShingle Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane
Regenhardt, Silvina Andrea
LACTOSE
ENZYMATIC HYDROLYSIS
MEMBRANE BIOREACTOR
WHEY
title_short Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane
title_full Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane
title_fullStr Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane
title_full_unstemmed Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane
title_sort Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane
dc.creator.none.fl_str_mv Regenhardt, Silvina Andrea
Mammarella, Enrique José
Rubiolo, Amelia Catalina
author Regenhardt, Silvina Andrea
author_facet Regenhardt, Silvina Andrea
Mammarella, Enrique José
Rubiolo, Amelia Catalina
author_role author
author2 Mammarella, Enrique José
Rubiolo, Amelia Catalina
author2_role author
author
dc.subject.none.fl_str_mv LACTOSE
ENZYMATIC HYDROLYSIS
MEMBRANE BIOREACTOR
WHEY
topic LACTOSE
ENZYMATIC HYDROLYSIS
MEMBRANE BIOREACTOR
WHEY
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv In this study, ß-galactosidase enzyme from Kluyveromyces fragilis was immobilised on a commercial polyethersulfone membrane surface, 10 kDa cut-off. An integrated process, concerning the simultaneous hydrolysis–ultrafiltration of whey lactose was studied and working conditions have been fixed at 55°C and pH 6.9, the same conditions that are used for the industrial process of protein concentration. For the immobilisation, best results were obtained using 5% (v/v) of glutaraldehyde solution and 0.03 M galactose; the total activity recovery coefficient (TARC) was 44.2%. The amount of immobilised enzyme was 12.49 mg with a total activity of 86.3 LAU at 37°C, using 5% (w/v) lactose solution in phosphate buffer (100 mM pH 6.9). The stability of the immobilised enzyme was approximately 585 fold higher in comparison with the stability of free enzyme. Multipoint covalent immobilisation improves the stability of the enzyme, thereby enhancing the decision to use the membrane as a filtering element and support for the enzyme immobilisation.
Fil: Regenhardt, Silvina Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico Para la Industria Química (i); Argentina
Fil: Mammarella, Enrique José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico Para la Industria Química (i); Argentina
Fil: Rubiolo, Amelia Catalina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico Para la Industria Química (i); Argentina
description In this study, ß-galactosidase enzyme from Kluyveromyces fragilis was immobilised on a commercial polyethersulfone membrane surface, 10 kDa cut-off. An integrated process, concerning the simultaneous hydrolysis–ultrafiltration of whey lactose was studied and working conditions have been fixed at 55°C and pH 6.9, the same conditions that are used for the industrial process of protein concentration. For the immobilisation, best results were obtained using 5% (v/v) of glutaraldehyde solution and 0.03 M galactose; the total activity recovery coefficient (TARC) was 44.2%. The amount of immobilised enzyme was 12.49 mg with a total activity of 86.3 LAU at 37°C, using 5% (w/v) lactose solution in phosphate buffer (100 mM pH 6.9). The stability of the immobilised enzyme was approximately 585 fold higher in comparison with the stability of free enzyme. Multipoint covalent immobilisation improves the stability of the enzyme, thereby enhancing the decision to use the membrane as a filtering element and support for the enzyme immobilisation.
publishDate 2013
dc.date.none.fl_str_mv 2013-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/8866
Regenhardt, Silvina Andrea; Mammarella, Enrique José; Rubiolo, Amelia Catalina; Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane; Versita; Chemical And Process Engineering-inzynieria Chemiczna I Procesowa; 34; 3; 10-2013; 375-385
2300-1925
url http://hdl.handle.net/11336/8866
identifier_str_mv Regenhardt, Silvina Andrea; Mammarella, Enrique José; Rubiolo, Amelia Catalina; Hydrolysis of lactose from cheese whey using a reactor with beta-galactosidase enzyme immobilized on a commercial UF membrane; Versita; Chemical And Process Engineering-inzynieria Chemiczna I Procesowa; 34; 3; 10-2013; 375-385
2300-1925
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.2478/cpe-2013-0030
info:eu-repo/semantics/altIdentifier/url/https://www.degruyter.com/view/j/cpe.2013.34.issue-3/cpe-2013-0030/cpe-2013-0030.xml
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Versita
publisher.none.fl_str_mv Versita
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846083439715942400
score 13.22299

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