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Effect of ethyleneoxide groups of anionic surfactants on lipase activity

2016-10Journal article Restricted access
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dc.contributor.authorMagalhães, Solange S.
dc.contributor.authorAlves, Luis
dc.contributor.authorSebastião, Marco
dc.contributor.authorMedronho, Bruno
dc.contributor.authorAlmeida, Zaida L.
dc.contributor.authorFaria, Tiago Q.
dc.contributor.authorBrito, Rui M. M.
dc.contributor.authorMoreno, Maria J.
dc.contributor.authorAntunes, Filipe E.
dc.date.accessioned2017-04-07T15:56:03Z
dc.date.available2017-04-07T15:56:03Z
dc.date.issued2016-10
dc.description.abstractThe use of enzymes in laundry and dish detergent products is growing. Such tendency implies dedicated studies to understand surfactant-enzyme interactions. The interactions between surfactants and enzymes and their impact on the catalytic efficiency represent a central problem and were here evaluated using circular dichroism, dynamic light scattering, and enzyme activity determinations. This work focuses on this key issue by evaluating the role of the ethyleneoxide (EO) groups of anionic surfactants on the structure and activity of a commercial lipase, and by focusing on the protein/surfactant interactions at a molecular level. The conformational changes and enzymatic activity of the protein were evaluated in the presence of sodium dodecyl sulfate (SDS also denoted as SLE0S) and of sodium lauryl ether sulfate with two EO units (SLE2S). The results strongly suggest that the presence of EO units in the surfactant polar headgroup determines the stability and the activity of the enzyme. While SDS promotes enzyme denaturation and consequent loss of activity, SLE2S preserves the enzyme structure and activity. The data further highlights that the electrostatic interactions among the protein groups are changed by the presence of the adsorbed anionic surfactants being such absorption mainly driven by hydrophobic interactions. (c) 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:1276-1282, 2016
dc.identifier.doi10.1002/btpr.2310
dc.identifier.issn8756-7938
dc.identifier.urihttp://hdl.handle.net/10400.1/9301
dc.language.isoeng
dc.peerreviewedyes
dc.relationDevelopment of sustainable processes for the production of textile fibers from forest resources
dc.relationEFFICIENT LOW-COST GELS OF CROSS-LINKED POLYELECTROLYTES OR CELLULOSE
dc.relation.isbasedonWOS:000387787600021
dc.titleEffect of ethyleneoxide groups of anionic surfactants on lipase activity
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleDevelopment of sustainable processes for the production of textile fibers from forest resources
oaire.awardTitleEFFICIENT LOW-COST GELS OF CROSS-LINKED POLYELECTROLYTES OR CELLULOSE
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FAGR-TEC%2F4049%2F2012/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F80556%2F2011/PT
oaire.citation.endPage1282
oaire.citation.issue5
oaire.citation.startPage1276
oaire.citation.titleBiotechnology Progress
oaire.citation.volume32
oaire.fundingStream3599-PPCDT
person.familyNameMedronho
person.givenNameBruno
person.identifier.ciencia-id6918-9AB3-8D22
person.identifier.orcid0000-0003-0972-1739
person.identifier.ridP-5927-2014
person.identifier.scopus-author-id9940656700
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
rcaap.rightsrestrictedAccess
rcaap.typearticle
relation.isAuthorOfPublication4c03571a-93da-4504-8acf-c74326449852
relation.isAuthorOfPublication.latestForDiscovery4c03571a-93da-4504-8acf-c74326449852
relation.isProjectOfPublication9b5cf26e-5e4f-404e-9128-dbe3f03582c7
relation.isProjectOfPublication10dff2c2-67db-4248-9ac8-d8b653f5b3ec
relation.isProjectOfPublication.latestForDiscovery9b5cf26e-5e4f-404e-9128-dbe3f03582c7

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