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http://hdl.handle.net/10261/186596
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Dos Santos, José C. S. | - |
dc.contributor.author | García-Galán, Cristina | - |
dc.contributor.author | Rodrigues, Rafael C. | - |
dc.contributor.author | Batista de Sant’Ana, Hosiberto | - |
dc.contributor.author | Gonçalves, Luciana R. B. | - |
dc.contributor.author | Fernández-Lafuente, Roberto | - |
dc.date.accessioned | 2019-07-23T09:58:48Z | - |
dc.date.available | 2019-07-23T09:58:48Z | - |
dc.date.issued | 2014-09 | - |
dc.identifier.citation | Process Biochemistry 49(9): 1511-1515 (2014) | - |
dc.identifier.issn | 1359-5113 | - |
dc.identifier.uri | http://hdl.handle.net/10261/186596 | - |
dc.description.abstract | Lecitase Ultra has been covalently immobilized on cyanogen bromide cross-linked 4% agarose (CNBr) beads, maintaining 70% of the initial activity. The activity of the immobilized enzyme was improved in the presence of Triton X-100, sodium dodecyl sulfate (SDS), and cetyltrimethyl ammonium bromide (CTAB) (e.g., up to 800% when using CTAB). However, CTAB and Triton X-100 presented a negative effect on enzyme stability even at low concentrations, and SDS cannot be used for a long time at 1% concentration. To maintain the hyperactivated conformation of the enzyme in the absence of detergent, ionic polymers were added during incubation of the immobilized enzyme in the presence of detergents. Coating the immobilized enzyme with polyethylenimine in aqueous buffer (PEI) produced a 3-fold increase in enzyme activity. However, in the presence of 0.1% SDS (v/v), this coating produced a 50-fold increase in enzyme activity. Using PEI and 0.01% (v/v) CTAB, the Lecitase activity decreased to 10%. Using irreversible inhibitors, it could be shown that the PEI/SDS-CNBr-Lecitase preparation allowed its catalytic Ser to be more accessible to the reaction medium than the unmodified CNBr-Lecitase. | - |
dc.description.sponsorship | We gratefully recognize the support from the Spanish Government, grant numbers CTQ2009-07568 and CTQ2013-41507-R and CNPq (Brazil). The predoctoral fellowships for Ms. García-Galán (Spanish Government) and Mr. dos Santos (CNPq, Brazil) are also recognized. | - |
dc.publisher | Elsevier | - |
dc.relation | info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/CTQ2013-41507-R | - |
dc.rights | closedAccess | - |
dc.subject | Bioimprinting | - |
dc.subject | Detergents | - |
dc.subject | PEISolid-phase physical modification | - |
dc.subject | Enzyme hyperactivation | - |
dc.subject | Lecitase | - |
dc.title | Stabilizing hyperactivated lecitase structures through physical treatment with ionic polymers | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1016/j.procbio.2014.05.009 | - |
dc.relation.publisherversion | https://doi.org/10.1016/j.procbio.2014.05.009 | - |
dc.date.updated | 2019-07-23T09:58:48Z | - |
dc.description.version | Peer Reviewed | - |
dc.language.rfc3066 | eng | - |
dc.contributor.funder | Ministerio de Economía y Competitividad (España) | - |
dc.contributor.funder | Ministerio de Ciencia e Innovación (España) | - |
dc.contributor.funder | Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil) | - |
dc.relation.csic | Sí | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100004837 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003329 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003593 | es_ES |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.grantfulltext | none | - |
item.fulltext | No Fulltext | - |
item.openairetype | artículo | - |
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