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Production, purification and characterization of laccase from pleurottus ostreatus grown on tomato pomace

2012-01Artigo científico Acesso restrito
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dc.contributor.authorFreixo, Maria do Rosário
dc.contributor.authorKarmali, Amin
dc.contributor.authorArteiro, José Maria Santos
dc.date.accessioned2015-09-08T15:13:08Z
dc.date.available2015-09-08T15:13:08Z
dc.date.issued2012-01
dc.description.abstractA strain of Pleurotus ostreatus was grown in tomato pomace as sole carbon source for production of laccase. The culture of P. ostreatus revealed a peak of laccase activity (147 U/L of fermentation broth) on the 4th day of culture with a specific activity of 2.8 U/mg protein. Differential chromatographic behaviour of laccase was investigated on affinity chromatographic matrices containing either urea, acetamide, ethanolamine or IDA as affinity ligands. Laccase exhibited retention on such affinity matrices and it was purified on a Sepharose 6B-BDGE-urea column with final enzyme recoveries of about 60%, specific activity of 6.0 and 18.0 U/mg protein and purification factors in the range of 14-46. It was also possible to demonstrate that metal-free laccase did not adsorb to Sepharose 6B-BDGE-urea column which suggests that adsorption of native laccase on this affinity matrix was apparently due to the specific interaction of carbonyl groups available on the matrix with the active site Cu (II) ions of laccase. The kinetic parameters (V (max), K (m) , K (cat), and K (cat)/K (m) ) of the purified enzyme for several substrates were determined as well as laccase stability and optimum pH and temperature of enzyme activity. This is the first report describing the production of laccase from P. ostreatus grown on tomato pomace and purification of this enzyme based on affinity matrix containing urea as affinity ligand.por
dc.identifier.citationFREIXO, M. do R.; KARMALI, A.; ARTEIRO, J. M. – Production, purification and characterization of laccase from pleurottus ostreatus grown on tomato pomace. World Journal of Microbiology & Biotechnology. ISSN: 0959-3993. Vol. 28, nr. 1 (2012), pp. 245-254por
dc.identifier.doi10.1007/s11274-011-0813-4
dc.identifier.issn0959-3993
dc.identifier.urihttp://hdl.handle.net/10400.21/5116
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherSpringerpor
dc.relationFundação para a Ciência e Tecnologia - POCTI/EQU/48812/2002
dc.relationÉvora University
dc.subjectLaccase from Pleurotus Ostreatuspor
dc.subjectLignocellulosic Enzymespor
dc.subjectAffinity Chromatographypor
dc.subjectReverse IMACpor
dc.subjectEpoxy-Activated Sepharose 6B-ureapor
dc.subjectTomato Pomacepor
dc.subjectChromatographic behavior
dc.subjectAffinity-chromatography
dc.subjectPseudomonas-aeruginosa
dc.subjectVersicolor
dc.subjectXylanase
dc.subjectAdsorption
dc.subjectIndustrial
dc.subjectStrains
dc.subjectAmidades
dc.subjectLignin
dc.titleProduction, purification and characterization of laccase from pleurottus ostreatus grown on tomato pomacepor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.conferencePlaceNew York
oaire.citation.endPage254por
oaire.citation.issue1por
oaire.citation.startPage245por
oaire.citation.titleWorld Journal of Microbiology & Biotechnologypor
oaire.citation.volume28por
person.familyNameKarmali
person.givenNameAmin
person.identifier.orcid0000-0003-0419-401X
person.identifier.ridE-4787-2011
person.identifier.scopus-author-id6603778216
rcaap.rightsclosedAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublication23975b4b-3234-4139-9675-89ea6f9a2332
relation.isAuthorOfPublication.latestForDiscovery23975b4b-3234-4139-9675-89ea6f9a2332

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ISEL - Eng. Quim. Biol. - Artigos