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
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/101211

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spelling 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
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info:eu-repo/semantics/publishedVersion
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status_str publishedVersion
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dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/15497852
info:eu-repo/semantics/altIdentifier/doi/10.1080/10408398.2020.1783639
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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)
eu_rights_str_mv openAccess
rights_invalid_str_mv 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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instname:Universidad Nacional de La Plata
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reponame_str SEDICI (UNLP)
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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