Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking
- Autores
- Martín, María Carolina; Lopez, Olivia Valeria; Ciolino, Andrés Eduardo; Morata, Vilma Ines; Villar, Marcelo Armando; Ninago, Mario Daniel
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- A biocatalyst was obtained by immobilizing an enological commercial pectinase within calcium alginate hydrogels using an entrapment technique, and its catalytic activity was evaluated during different storage conditions. Hydrogel beads were stored at 4 °C in three different ways: (i) wet, in citrate buffer solution (pH 3.8); (ii) dehydrated by using a vacuum stove; and (iii) freeze-dried. Biocatalyst surface and their internal morphology were characterized by Scanning Electron Microscopy and a good enzyme distribution throughout alginate matrix was observed. Fourier Transform Infrared Spectroscopy results confirmed the presence of absorption bands associated with amino groups present in enzymes. Immobilization procedure did not modify the optimal pH and temperature (pH = 4.0 and 20 °C) for pectinase activity, comparing to free enzyme. Entrapped pectinase showed activity until six reaction cycles with 40% residual activity. Storage stability studies demonstrated that wet entrapped pectinase retained its initial enzymatic activity up to 11 weeks, whereas that lyophilized hydrogels retained its original activity after 8 months of storage. These results suggest that immobilized pectinase may be successfully exploited in various industrial applications, with special concern in grape juice clarification process. Thus, the turbidity of grape must decreased significantly using the immobilized pectinase during 150 min at 20 °C. This biocatalyst could be easily removed after clarification process and it can be reused, minimizing production economic costs in wine industry.
Fil: Martín, María Carolina. Universidad Nacional de Cuyo. Facultad de Ciencias Aplicadas a la Industria; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina
Fil: Lopez, Olivia Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Ciolino, Andrés Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Morata, Vilma Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Aplicadas a la Industria; Argentina
Fil: Villar, Marcelo Armando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Ninago, Mario Daniel. Universidad Nacional de Cuyo. Facultad de Ciencias Aplicadas a la Industria; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina - Materia
-
BIOCATALYST
CALCIUM ALGINATE HYDROGELS
PECTINASE IMMOBILIZATION
WINEMAKING - 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:11336/99443
Ver los metadatos del registro completo
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Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemakingMartín, María CarolinaLopez, Olivia ValeriaCiolino, Andrés EduardoMorata, Vilma InesVillar, Marcelo ArmandoNinago, Mario DanielBIOCATALYSTCALCIUM ALGINATE HYDROGELSPECTINASE IMMOBILIZATIONWINEMAKINGhttps://purl.org/becyt/ford/2.5https://purl.org/becyt/ford/2A biocatalyst was obtained by immobilizing an enological commercial pectinase within calcium alginate hydrogels using an entrapment technique, and its catalytic activity was evaluated during different storage conditions. Hydrogel beads were stored at 4 °C in three different ways: (i) wet, in citrate buffer solution (pH 3.8); (ii) dehydrated by using a vacuum stove; and (iii) freeze-dried. Biocatalyst surface and their internal morphology were characterized by Scanning Electron Microscopy and a good enzyme distribution throughout alginate matrix was observed. Fourier Transform Infrared Spectroscopy results confirmed the presence of absorption bands associated with amino groups present in enzymes. Immobilization procedure did not modify the optimal pH and temperature (pH = 4.0 and 20 °C) for pectinase activity, comparing to free enzyme. Entrapped pectinase showed activity until six reaction cycles with 40% residual activity. Storage stability studies demonstrated that wet entrapped pectinase retained its initial enzymatic activity up to 11 weeks, whereas that lyophilized hydrogels retained its original activity after 8 months of storage. These results suggest that immobilized pectinase may be successfully exploited in various industrial applications, with special concern in grape juice clarification process. Thus, the turbidity of grape must decreased significantly using the immobilized pectinase during 150 min at 20 °C. This biocatalyst could be easily removed after clarification process and it can be reused, minimizing production economic costs in wine industry.Fil: Martín, María Carolina. Universidad Nacional de Cuyo. Facultad de Ciencias Aplicadas a la Industria; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; ArgentinaFil: Lopez, Olivia Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaFil: Ciolino, Andrés Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaFil: Morata, Vilma Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Aplicadas a la Industria; ArgentinaFil: Villar, Marcelo Armando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaFil: Ninago, Mario Daniel. Universidad Nacional de Cuyo. Facultad de Ciencias Aplicadas a la Industria; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; ArgentinaElsevier2019-03info: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/11336/99443Martín, María Carolina; Lopez, Olivia Valeria; Ciolino, Andrés Eduardo; Morata, Vilma Ines; Villar, Marcelo Armando; et al.; Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking; Elsevier; Biocatalysis and Agricultural Biotechnology; 18; 3-2019; 1-43; 1010911878-8181CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcab.2019.101091info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S187881811831020Xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:10:54Zoai:ri.conicet.gov.ar:11336/99443instacron: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 10:10:54.4CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking |
title |
Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking |
spellingShingle |
Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking Martín, María Carolina BIOCATALYST CALCIUM ALGINATE HYDROGELS PECTINASE IMMOBILIZATION WINEMAKING |
title_short |
Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking |
title_full |
Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking |
title_fullStr |
Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking |
title_full_unstemmed |
Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking |
title_sort |
Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking |
dc.creator.none.fl_str_mv |
Martín, María Carolina Lopez, Olivia Valeria Ciolino, Andrés Eduardo Morata, Vilma Ines Villar, Marcelo Armando Ninago, Mario Daniel |
author |
Martín, María Carolina |
author_facet |
Martín, María Carolina Lopez, Olivia Valeria Ciolino, Andrés Eduardo Morata, Vilma Ines Villar, Marcelo Armando Ninago, Mario Daniel |
author_role |
author |
author2 |
Lopez, Olivia Valeria Ciolino, Andrés Eduardo Morata, Vilma Ines Villar, Marcelo Armando Ninago, Mario Daniel |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
BIOCATALYST CALCIUM ALGINATE HYDROGELS PECTINASE IMMOBILIZATION WINEMAKING |
topic |
BIOCATALYST CALCIUM ALGINATE HYDROGELS PECTINASE IMMOBILIZATION WINEMAKING |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.5 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
A biocatalyst was obtained by immobilizing an enological commercial pectinase within calcium alginate hydrogels using an entrapment technique, and its catalytic activity was evaluated during different storage conditions. Hydrogel beads were stored at 4 °C in three different ways: (i) wet, in citrate buffer solution (pH 3.8); (ii) dehydrated by using a vacuum stove; and (iii) freeze-dried. Biocatalyst surface and their internal morphology were characterized by Scanning Electron Microscopy and a good enzyme distribution throughout alginate matrix was observed. Fourier Transform Infrared Spectroscopy results confirmed the presence of absorption bands associated with amino groups present in enzymes. Immobilization procedure did not modify the optimal pH and temperature (pH = 4.0 and 20 °C) for pectinase activity, comparing to free enzyme. Entrapped pectinase showed activity until six reaction cycles with 40% residual activity. Storage stability studies demonstrated that wet entrapped pectinase retained its initial enzymatic activity up to 11 weeks, whereas that lyophilized hydrogels retained its original activity after 8 months of storage. These results suggest that immobilized pectinase may be successfully exploited in various industrial applications, with special concern in grape juice clarification process. Thus, the turbidity of grape must decreased significantly using the immobilized pectinase during 150 min at 20 °C. This biocatalyst could be easily removed after clarification process and it can be reused, minimizing production economic costs in wine industry. Fil: Martín, María Carolina. Universidad Nacional de Cuyo. Facultad de Ciencias Aplicadas a la Industria; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina Fil: Lopez, Olivia Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina Fil: Ciolino, Andrés Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina Fil: Morata, Vilma Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Aplicadas a la Industria; Argentina Fil: Villar, Marcelo Armando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina Fil: Ninago, Mario Daniel. Universidad Nacional de Cuyo. Facultad de Ciencias Aplicadas a la Industria; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina |
description |
A biocatalyst was obtained by immobilizing an enological commercial pectinase within calcium alginate hydrogels using an entrapment technique, and its catalytic activity was evaluated during different storage conditions. Hydrogel beads were stored at 4 °C in three different ways: (i) wet, in citrate buffer solution (pH 3.8); (ii) dehydrated by using a vacuum stove; and (iii) freeze-dried. Biocatalyst surface and their internal morphology were characterized by Scanning Electron Microscopy and a good enzyme distribution throughout alginate matrix was observed. Fourier Transform Infrared Spectroscopy results confirmed the presence of absorption bands associated with amino groups present in enzymes. Immobilization procedure did not modify the optimal pH and temperature (pH = 4.0 and 20 °C) for pectinase activity, comparing to free enzyme. Entrapped pectinase showed activity until six reaction cycles with 40% residual activity. Storage stability studies demonstrated that wet entrapped pectinase retained its initial enzymatic activity up to 11 weeks, whereas that lyophilized hydrogels retained its original activity after 8 months of storage. These results suggest that immobilized pectinase may be successfully exploited in various industrial applications, with special concern in grape juice clarification process. Thus, the turbidity of grape must decreased significantly using the immobilized pectinase during 150 min at 20 °C. This biocatalyst could be easily removed after clarification process and it can be reused, minimizing production economic costs in wine industry. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-03 |
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/11336/99443 Martín, María Carolina; Lopez, Olivia Valeria; Ciolino, Andrés Eduardo; Morata, Vilma Ines; Villar, Marcelo Armando; et al.; Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking; Elsevier; Biocatalysis and Agricultural Biotechnology; 18; 3-2019; 1-43; 101091 1878-8181 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/99443 |
identifier_str_mv |
Martín, María Carolina; Lopez, Olivia Valeria; Ciolino, Andrés Eduardo; Morata, Vilma Ines; Villar, Marcelo Armando; et al.; Immobilization of enological pectinase in calcium alginate hydrogels: A potential biocatalyst for winemaking; Elsevier; Biocatalysis and Agricultural Biotechnology; 18; 3-2019; 1-43; 101091 1878-8181 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcab.2019.101091 info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S187881811831020X |
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 |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
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_ |
1844614002393481216 |
score |
13.070432 |