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Bacterial laccases: some recent advances and applications

2020-08Book part Open access
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dc.contributor.authorMartins, Lígia O.
dc.contributor.authorMelo, Eduardo P.
dc.contributor.authorSanchez-Amat, Antonio
dc.contributor.authorRobalo, Maria Paula
dc.date.accessioned2023-02-03T12:51:53Z
dc.date.available2023-02-03T12:51:53Z
dc.date.issued2020-08
dc.description.abstractLaccases belong to the large family of multi-copper oxidases (MCOs) that couple the one-electron oxidation of substrates with the four-electron reduction of molecular oxygen to water. Because of their high relative non-specific oxidation capacity particularly on phenols and aromatic amines as well as the lack of requirement for expensive organic cofactors, they have found application in a large number of biotechnological fields. The vast majority of studies and applications were performed using fungal laccases, but bacterial laccases show interesting properties such as optimal temperature above 50 °C, optimal pH at the neutral to alkaline range, thermal and chemical stability and increased salt tolerance. Additionally, bacterial systems benefit from a wide range of molecular biology tools that facilitates their engineering and achievement of high yields of protein production and set-up of cost-effective bioprocesses. In this review we will provide up-to-date information on the distribution and putative physiological role of bacterial laccases and highlight their distinctive structural and biochemical properties, discuss the key role of copper in the biochemical properties, discuss thermostability determinants and, finally, review biotechnological applications with a focus on catalytic mechanisms on phenolics and aromatic amines.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationMARTINS, Lígia O.; MELO, Eduardo Pinho.; SANCHEZ-AMAT, Antonio; ROBALO, Maria Paula. - Bacterial Laccases: Some Recent Advances and Applications In Laccases in Bioremediation and Waste Valorisation. Vol. 33, Springer, 2020, ISBN: 978-3-030-47906-0. p.1-25pt_PT
dc.identifier.doi10.1007/978-3-030-47906-0_2pt_PT
dc.identifier.isbn978-3-030-47906-0
dc.identifier.urihttp://hdl.handle.net/10400.21/15477
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherSpringerpt_PT
dc.relation01-0145-FEDER-007660pt_PT
dc.relationGA 824017pt_PT
dc.relationBioresources 4 Sustainability
dc.relationCentro de Química Estrutural
dc.relation.publisherversionhttps://link.springer.com/chapter/10.1007/978-3-030-47906-0_2pt_PT
dc.subjectPhylogenetic analysispt_PT
dc.subjectMulti-copper oxidasespt_PT
dc.subjectMetallo-oxidasespt_PT
dc.subjectStructure-functionpt_PT
dc.subjectProtein stabilitypt_PT
dc.subjectBiocatalysispt_PT
dc.subjectOxidative bioprocessespt_PT
dc.subjectHomocoupling reactionspt_PT
dc.titleBacterial laccases: some recent advances and applicationspt_PT
dc.typebook part
dspace.entity.typePublication
oaire.awardTitleBioresources 4 Sustainability
oaire.awardTitleCentro de Química Estrutural
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBBB-EBB%2F0122%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/9471 - RIDTI/PTDC%2FBII-BBF%2F29564%2F2017/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UID%2FMulti%2F04551%2F2013/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UID%2FQUI%2F00100%2F2013/PT
oaire.citation.endPage25pt_PT
oaire.citation.startPage1pt_PT
oaire.citation.titleLaccases in Bioremediation and Waste Valorisationpt_PT
oaire.citation.volume33pt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStream9471 - RIDTI
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
person.familyNameMartins
person.familyNamePinho Melo
person.familyNameSanchez-Amat
person.familyNameRobalo
person.givenNameLígia O.
person.givenNameEduardo
person.givenNameAntonio
person.givenNameMaria Paula
person.identifier319225
person.identifier.ciencia-id731B-B843-C1DF
person.identifier.ciencia-id3C1C-C10C-1510
person.identifier.ciencia-idE11C-A704-9C18
person.identifier.orcid0000-0003-0082-9591
person.identifier.orcid0000-0002-0974-8977
person.identifier.orcid0000-0001-8597-9235
person.identifier.orcid0000-0002-8200-6910
person.identifier.ridC-2513-2009
person.identifier.ridL-2695-2014
person.identifier.ridB-2002-2012
person.identifier.scopus-author-id7102109314
person.identifier.scopus-author-id9269662100
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typebookPartpt_PT
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