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Recent advances in β-galactosidase and fructosyltransferase immobilization technology

2020Journal article Open access
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dc.contributor.authorUreta, Maria Micaela
dc.contributor.authorMartins, Gonçalo Nuno
dc.contributor.authorFigueira, Onofre
dc.contributor.authorPires, Pedro Filipe
dc.contributor.authorCastilho, Paula Cristina
dc.contributor.authorGomez-Zavaglia, Andrea
dc.date.accessioned2022-09-30T10:26:25Z
dc.date.available2022-09-30T10:26:25Z
dc.date.issued2020
dc.description.abstractThe 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 pro mote 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 proc esses with special care on those reported for two types of enzymes: b-galactosidases and fructo syltransferases. 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 b-galactosidases and fructosyltransferases, but there is still great place for innovative developments.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationFilipe Pires, Paula Cristina Castilho & Andrea Gomez-Zavaglia (2021) Recent advances in β galactosidase and fructosyltransferase immobilization technology, Critical Reviews in Food Science and Nutrition, 61:16, 2659-2690, DOI: 10.1080/10408398.2020.1783639pt_PT
dc.identifier.doi10.1080/10408398.2020.1783639pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.13/4675
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherTaylor and Francis Grouppt_PT
dc.relationStrategic Project - UI 674 - 2014
dc.relation.publisherversionhttps://doi.org/10.1080/10408398.2020.1783639pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/pt_PT
dc.subjectb-galactosidasept_PT
dc.subjectImmobilization methodspt_PT
dc.subjectFructosyltransferasept_PT
dc.subjectSupportspt_PT
dc.subject.pt_PT
dc.subjectFaculdade de Ciências Exatas e da Engenhariapt_PT
dc.subjectCentro de Química da Madeira
dc.titleRecent advances in β-galactosidase and fructosyltransferase immobilization technologypt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleStrategic Project - UI 674 - 2014
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/PEst-OE%2FQUI%2FUI0674%2F2014/PT
oaire.citation.endPage2690pt_PT
oaire.citation.issue16pt_PT
oaire.citation.startPage2659pt_PT
oaire.citation.titleCritical Reviews in Food Science and Nutritionpt_PT
oaire.citation.volume61pt_PT
oaire.fundingStream6817 - DCRRNI ID
person.familyNameUreta
person.familyNameMartins
person.familyNameFigueira
person.familyNameDuarte Louzeiro Pires
person.familyNameCastilho
person.familyNameGomez-Zavaglia
person.givenNameMicaela
person.givenNameGonçalo
person.givenNameOnofre
person.givenNamePedro Filipe
person.givenNamePaula C
person.givenNameAndrea
person.identifier741627
person.identifierC-3387-2012
person.identifierA-4412-2013
person.identifier252190
person.identifier.ciencia-idE317-F805-6C98
person.identifier.ciencia-idDC1F-D018-160E
person.identifier.ciencia-idD413-1517-1263
person.identifier.ciencia-id6D15-8C69-A2E0
person.identifier.ciencia-idCE1B-CEE0-250F
person.identifier.orcid0000-0003-1390-6429
person.identifier.orcid0000-0002-1869-6208
person.identifier.orcid0000-0001-5732-0994
person.identifier.orcid0000-0001-8583-7990
person.identifier.orcid0000-0002-8303-4286
person.identifier.orcid0000-0002-8705-0160
person.identifier.scopus-author-id57209466494
person.identifier.scopus-author-id7003655474
person.identifier.scopus-author-id6602189336
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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