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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/8866
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T10:32:41Zoai: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:34982025-09-29 10:32:41.772CONICET 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 |
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1844614341349867520 |
score |
13.070432 |