Utilize este identificador para referenciar este registo:
https://hdl.handle.net/1822/44995
Registo completo
Campo DC | Valor | Idioma |
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dc.contributor.author | Wanderley, M. | por |
dc.contributor.author | Neto, José Manoel Wanderley Duarte | por |
dc.contributor.author | Albuquerque, Wendell Wagner Campos | por |
dc.contributor.author | Marques, Daniela de Araújo Viana | por |
dc.contributor.author | Lima, Carolina de Albuquerque | por |
dc.contributor.author | Silvério, Sara C. | por |
dc.contributor.author | Filho, José Luiz de Lima | por |
dc.contributor.author | Teixeira, J. A. | por |
dc.contributor.author | Porto, Ana Lúcia Figueiredo | por |
dc.date.accessioned | 2017-03-13T19:49:30Z | - |
dc.date.available | 2017-03-13T19:49:30Z | - |
dc.date.issued | 2017-05 | - |
dc.identifier.citation | Wanderley, M.; Neto, José Manoel Wanderley Duarte; Albuquerque, Wendell Wagner Campos; Marques, Daniela de Araújo Viana; Lima, Carolina de Albuquerque; Silvério, Sara C.; Filho, José Luiz de Lima; Teixeira, J. A.; Porto, Ana Lúcia Figueiredo, Purification and characterization of a collagenase from Penicillium sp. UCP 1286 by polyethylene glycol-phosphate aqueous two-phase system. Protein Expression and Purification, 133, 8-14, 2017 | por |
dc.identifier.issn | 1046-5928 | por |
dc.identifier.uri | https://hdl.handle.net/1822/44995 | - |
dc.description.abstract | Collagenases are proteolytic enzymes capable of degrading both native and denatured collagen, reported to be applied in industrial, medical and biotechnological sectors. Liquid-liquid extraction using aqueous two-phase system (ATPS) is one of the most promising bioseparation techniques, which can substitute difficult solid-liquid separation processes, offering many advantages over conventional methods including low-processing time, low-cost material and low-energy consumption. The collagenase produced by Penicillium sp. UCP 1286 showed a stronger affinity for the bottom salt-rich phase, where the highest levels of collagenolytic activity were observed at the center point runs, using 15.0% (w/w) PEG 3350 g/mol and 12.5% (w/w) phosphate salt at pH 7.0 and concentration. The enzyme was characterized by thermal stability, pH tolerance and effect of inhibitors, showing optimal collagenolytic activity at 37 °C and pH 9.0 and proved to be a serine protease. ATPS showed high efficiency in the collagenase purification, confirmed by a single band in SDS/PAGE, and can in fact be applied as a quick and inexpensive alternative method. | por |
dc.description.sponsorship | This work was supported by the National Council of Technological and Scientific Development (CNPq) and Coordination for the Improvement of Higher Education Personnel (CAPES). Sara Silvério also acknowledges her post-doc grant (SFRH/BPD/88584/2012) from FCT (SFRH/BPD/88584/2012) (Portuguese Science and Technology Foundation), Portugal. | por |
dc.language.iso | eng | por |
dc.publisher | Elsevier 1 | por |
dc.relation | info:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBPD%2F88584%2F2012/PT | por |
dc.relation | info:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBPD%2F88584%2F2012/PT | por |
dc.rights | openAccess | por |
dc.subject | Collagenolytic enzyme | por |
dc.subject | Collagen | por |
dc.subject | ATPS | por |
dc.subject | Purification | por |
dc.title | Purification and characterization of a collagenase from Penicillium sp. UCP 1286 by polyethylene glycol-phosphate aqueous two-phase system | por |
dc.type | article | - |
dc.peerreviewed | yes | por |
dc.comments | CEB46694 | por |
sdum.publicationstatus | info:eu-repo/semantics/publishedVersion | por |
oaire.citationStartPage | 8 | por |
oaire.citationEndPage | 14 | por |
oaire.citationConferencePlace | United States | - |
oaire.citationTitle | Protein Expression and Purification | por |
oaire.citationVolume | 133 | por |
dc.date.updated | 2017-03-11T18:35:27Z | - |
dc.identifier.eissn | 1096-0279 | por |
dc.identifier.doi | 10.1016/j.pep.2017.02.010 | por |
dc.identifier.pmid | 28242427 | por |
dc.subject.wos | Science & Technology | por |
sdum.journal | Protein Expression and Purification | por |
Aparece nas coleções: | CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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document_46694_1.pdf | 449,21 kB | Adobe PDF | Ver/Abrir |