Enzyme Activity of Catalase Immobilized in Langmuir-Blodgett Films of Phospholipids

Enzyme Activity of Catalase Immobilized in Langmuir-Blodgett Films of Phospholipids

Author Goto, Thiago E. Autor UNIFESP Google Scholar
Lopez, Ricardo F. Autor UNIFESP Google Scholar
Oliveira, Osvaldo N. Google Scholar
Caseli, Luciano Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Abstract A major challenge for producing low cost biosensors based on nanostructured films with control of molecular architectures is to preserve the catalytic activity of the immobilized biomolecules. in this study, we show that catalase (HRP) keeps its activity if immobilized in Langmuir-Blodgett (LB) films of dipalmitoyl phosphatidylglycerol (DPPG). the incorporation of catalase into a DPPG monolayer at the at interface was demonstrated with surface pressure and surface potential isotherms, in addition to polarization-modulated infrared reflection absorption spectroscopy (PM-IRRAS). According to the PM-IRRAS data. catalase was not denatured upon adsorption on a preformed DPPG monolayer and could be transferred onto a solid substrate. the catalytic activity of catalase in a mixed LB film with DPPG was ca. 13% higher than in solution. the control of molecular architecture and choice of a suitable phospholipid matrix allows catalase-containing LB films to be used in sensing hydrogen peroxide.
Language English
Sponsor Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Date 2010-07-06
Published in Langmuir. Washington: Amer Chemical Soc, v. 26, n. 13, p. 11135-11139, 2010.
ISSN 0743-7463 (Sherpa/Romeo, impact factor)
Publisher Amer Chemical Soc
Extent 11135-11139
Origin http://dx.doi.org/10.1021/la101648x
Access rights Closed access
Type Article
Web of Science ID WOS:000279239900098
URI http://repositorio.unifesp.br/handle/11600/32721

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