Recent advances in β-galactosidase and fructosyltransferase immobilization technology
- Autores
- Ureta, María Micaela; Martins, Gonzalo Nuno; Figueira, Onofre; Pires, Pedro Filipe; Castilho, Paula Cristina; Gómez-Zavaglia, Andrea
- Año de publicación
- 2020
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The highly demanding conditions of industrial processes may lower the stability and affect the activity of enzymes used as biocatalysts. Enzyme immobilization emerged as an approach to promote stabilization and easy removal of enzymes for their reusability. The aim of this review is to go through the principal immobilization strategies addressed to achieve optimal industrial processes with special care on those reported for two types of enzymes: β-galactosidases and fructosyltransferases. The main methods used to immobilize these two enzymes are adsorption, entrapment, covalent coupling and cross-linking or aggregation (no support is used), all of them having pros and cons. Regarding the support, it should be cost-effective, assure the reusability and an easy recovery of the enzyme, increasing its stability and durability. The discussion provided showed that the type of enzyme, its origin, its purity, together with the type of immobilization method and the support will affect the performance during the enzymatic synthesis. Enzymes’ immobilization involves interdisciplinary knowledge including enzymology, nanotechnology, molecular dynamics, cellular physiology and process design. The increasing availability of facilities has opened a variety of possibilities to define strategies to optimize the activity and re-usability of β-galactosidases and fructosyltransferases, but there is still great place for innovative developments.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos - Materia
-
Ciencias Exactas
b-galactosidase
immobilization methods
fructosyltransferase
supports - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-nd/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/101211
Ver los metadatos del registro completo
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Recent advances in β-galactosidase and fructosyltransferase immobilization technologyUreta, María MicaelaMartins, Gonzalo NunoFigueira, OnofrePires, Pedro FilipeCastilho, Paula CristinaGómez-Zavaglia, AndreaCiencias Exactasb-galactosidaseimmobilization methodsfructosyltransferasesupportsThe highly demanding conditions of industrial processes may lower the stability and affect the activity of enzymes used as biocatalysts. Enzyme immobilization emerged as an approach to promote stabilization and easy removal of enzymes for their reusability. The aim of this review is to go through the principal immobilization strategies addressed to achieve optimal industrial processes with special care on those reported for two types of enzymes: β-galactosidases and fructosyltransferases. The main methods used to immobilize these two enzymes are adsorption, entrapment, covalent coupling and cross-linking or aggregation (no support is used), all of them having pros and cons. Regarding the support, it should be cost-effective, assure the reusability and an easy recovery of the enzyme, increasing its stability and durability. The discussion provided showed that the type of enzyme, its origin, its purity, together with the type of immobilization method and the support will affect the performance during the enzymatic synthesis. Enzymes’ immobilization involves interdisciplinary knowledge including enzymology, nanotechnology, molecular dynamics, cellular physiology and process design. The increasing availability of facilities has opened a variety of possibilities to define strategies to optimize the activity and re-usability of β-galactosidases and fructosyltransferases, but there is still great place for innovative developments.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2020-06-26info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/101211enginfo:eu-repo/semantics/altIdentifier/issn/15497852info:eu-repo/semantics/altIdentifier/doi/10.1080/10408398.2020.1783639info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:21:59Zoai:sedici.unlp.edu.ar:10915/101211Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:21:59.943SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Recent advances in β-galactosidase and fructosyltransferase immobilization technology |
title |
Recent advances in β-galactosidase and fructosyltransferase immobilization technology |
spellingShingle |
Recent advances in β-galactosidase and fructosyltransferase immobilization technology Ureta, María Micaela Ciencias Exactas b-galactosidase immobilization methods fructosyltransferase supports |
title_short |
Recent advances in β-galactosidase and fructosyltransferase immobilization technology |
title_full |
Recent advances in β-galactosidase and fructosyltransferase immobilization technology |
title_fullStr |
Recent advances in β-galactosidase and fructosyltransferase immobilization technology |
title_full_unstemmed |
Recent advances in β-galactosidase and fructosyltransferase immobilization technology |
title_sort |
Recent advances in β-galactosidase and fructosyltransferase immobilization technology |
dc.creator.none.fl_str_mv |
Ureta, María Micaela Martins, Gonzalo Nuno Figueira, Onofre Pires, Pedro Filipe Castilho, Paula Cristina Gómez-Zavaglia, Andrea |
author |
Ureta, María Micaela |
author_facet |
Ureta, María Micaela Martins, Gonzalo Nuno Figueira, Onofre Pires, Pedro Filipe Castilho, Paula Cristina Gómez-Zavaglia, Andrea |
author_role |
author |
author2 |
Martins, Gonzalo Nuno Figueira, Onofre Pires, Pedro Filipe Castilho, Paula Cristina Gómez-Zavaglia, Andrea |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Ciencias Exactas b-galactosidase immobilization methods fructosyltransferase supports |
topic |
Ciencias Exactas b-galactosidase immobilization methods fructosyltransferase supports |
dc.description.none.fl_txt_mv |
The highly demanding conditions of industrial processes may lower the stability and affect the activity of enzymes used as biocatalysts. Enzyme immobilization emerged as an approach to promote stabilization and easy removal of enzymes for their reusability. The aim of this review is to go through the principal immobilization strategies addressed to achieve optimal industrial processes with special care on those reported for two types of enzymes: β-galactosidases and fructosyltransferases. The main methods used to immobilize these two enzymes are adsorption, entrapment, covalent coupling and cross-linking or aggregation (no support is used), all of them having pros and cons. Regarding the support, it should be cost-effective, assure the reusability and an easy recovery of the enzyme, increasing its stability and durability. The discussion provided showed that the type of enzyme, its origin, its purity, together with the type of immobilization method and the support will affect the performance during the enzymatic synthesis. Enzymes’ immobilization involves interdisciplinary knowledge including enzymology, nanotechnology, molecular dynamics, cellular physiology and process design. The increasing availability of facilities has opened a variety of possibilities to define strategies to optimize the activity and re-usability of β-galactosidases and fructosyltransferases, but there is still great place for innovative developments. Centro de Investigación y Desarrollo en Criotecnología de Alimentos |
description |
The highly demanding conditions of industrial processes may lower the stability and affect the activity of enzymes used as biocatalysts. Enzyme immobilization emerged as an approach to promote stabilization and easy removal of enzymes for their reusability. The aim of this review is to go through the principal immobilization strategies addressed to achieve optimal industrial processes with special care on those reported for two types of enzymes: β-galactosidases and fructosyltransferases. The main methods used to immobilize these two enzymes are adsorption, entrapment, covalent coupling and cross-linking or aggregation (no support is used), all of them having pros and cons. Regarding the support, it should be cost-effective, assure the reusability and an easy recovery of the enzyme, increasing its stability and durability. The discussion provided showed that the type of enzyme, its origin, its purity, together with the type of immobilization method and the support will affect the performance during the enzymatic synthesis. Enzymes’ immobilization involves interdisciplinary knowledge including enzymology, nanotechnology, molecular dynamics, cellular physiology and process design. The increasing availability of facilities has opened a variety of possibilities to define strategies to optimize the activity and re-usability of β-galactosidases and fructosyltransferases, but there is still great place for innovative developments. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-06-26 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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http://sedici.unlp.edu.ar/handle/10915/101211 |
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http://sedici.unlp.edu.ar/handle/10915/101211 |
dc.language.none.fl_str_mv |
eng |
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eng |
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info:eu-repo/semantics/altIdentifier/issn/15497852 info:eu-repo/semantics/altIdentifier/doi/10.1080/10408398.2020.1783639 |
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info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-nd/4.0/ Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) |
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openAccess |
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http://creativecommons.org/licenses/by-nc-nd/4.0/ Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) |
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