Controlling the molecular architecture of lactase immobilized in Langmuir-Blodgett films of phospholipids to modulate the enzyme activity

Página do item simplificado
dc.citation.volume150
dc.contributor.authorAyoub, Fabio de Paula [UNIFESP]
dc.contributor.authorCaseli, Luciano [UNIFESP]
dc.coverageAmsterdam
dc.date.accessioned2020-07-17T14:03:10Z
dc.date.available2020-07-17T14:03:10Z
dc.date.issued2017
dc.description.abstractIn this present work, the adsorption of the enzyme lactase onto Langmuir monolayers of the phospholipid dimyristoylphosphatidic acid (DMPA) was investigated and characterized with surface pressure-area isotherms, surface potential-area isotherms and polarization-modulated infrared reflection-absorption spectroscopy (PM-IRRAS). The adsorption of the enzyme at the air-water interface expanded the lipid monolayer and increased the film compressibility at high surface pressures. Amide bands in the PM-IRRAS spectra were identified, with the C-N and C=O dipole moments lying parallel to the monolayer plane, revealing that the structuring of the enzyme into beta-sheets was kept in the mixed monolayer. The enzyme-lipid films were transferred from the floating monolayer to solid supports as Langmuir-Blodgett (LB) films and characterized with fluorescence spectroscopy and atomic force microscopy. The catalytic activity of the films was measured and compared to the homogenous medium. The enzyme accommodated in the LB films preserved more than 80% of the enzyme activity after 20 days, in contrast for the homogeneous medium, which preserved less than 60% of the enzyme activity. The method presented in this present work not only allows for an enhanced catalytic activity toward lactose, but also can help explain why certain film architectures exhibit better performance. (C) 2016 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Fed Sao Paulo, Inst Environm Chem & Pharmaceut Sci, Sao Paulo, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Inst Environm Chem & Pharmaceut Sci, Sao Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFAPESP
dc.description.sponsorshipCAPES fellowship
dc.description.sponsorshipIDFAPESP: 2015/23446-0
dc.description.sponsorshipIDFAPESP: 2014/12557-2
dc.format.extent8-14
dc.identifierhttp://dx.doi.org/10.1016/j.colsurfb.2016.11.015
dc.identifier.citationColloids And Surfaces B-Biointerfaces. Amsterdam, v. 150, p. 8-14, 2017.
dc.identifier.doi10.1016/j.colsurfb.2016.11.015
dc.identifier.issn0927-7765
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/55198
dc.identifier.wosWOS:000393726900002
dc.language.isoeng
dc.publisherElsevier Science Bv
dc.relation.ispartofColloids And Surfaces B-Biointerfaces
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectLactaseen
dc.subjectLangmuir monolayersen
dc.subjectLangmuir-Blodgett filmsen
dc.subjectBiosensorsen
dc.subjectEnzyme activityen
dc.titleControlling the molecular architecture of lactase immobilized in Langmuir-Blodgett films of phospholipids to modulate the enzyme activityen
dc.typeinfo:eu-repo/semantics/article
Arquivos
Coleções
ICAQF - Artigos