Recent advances in β-galactosidase and fructosyltransferase immobilization technology

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 th...

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Autores principales: Ureta, María Micaela, Martins, Gonzalo Nuno, Figueira, Onofre, Pires, Pedro Filipe, Castilho, Paula Cristina, Gómez-Zavaglia, Andrea
Formato: Articulo
Lenguaje:Inglés
Publicado: 2020
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/101211
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id I19-R120-10915-101211
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
b-galactosidase
immobilization methods
fructosyltransferase
supports
spellingShingle Ciencias Exactas
b-galactosidase
immobilization methods
fructosyltransferase
supports
Ureta, María Micaela
Martins, Gonzalo Nuno
Figueira, Onofre
Pires, Pedro Filipe
Castilho, Paula Cristina
Gómez-Zavaglia, Andrea
Recent advances in β-galactosidase and fructosyltransferase immobilization technology
topic_facet Ciencias Exactas
b-galactosidase
immobilization methods
fructosyltransferase
supports
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.
format Articulo
Articulo
author Ureta, María Micaela
Martins, Gonzalo Nuno
Figueira, Onofre
Pires, Pedro Filipe
Castilho, Paula Cristina
Gómez-Zavaglia, Andrea
author_facet Ureta, María Micaela
Martins, Gonzalo Nuno
Figueira, Onofre
Pires, Pedro Filipe
Castilho, Paula Cristina
Gómez-Zavaglia, Andrea
author_sort Ureta, María Micaela
title Recent advances in β-galactosidase and fructosyltransferase immobilization technology
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
publishDate 2020
url http://sedici.unlp.edu.ar/handle/10915/101211
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