Adsorption and enzyme activity of sucrose phosphorylase on lipid Langmuir and Langmuir-Blodgett films

Adsorption and enzyme activity of sucrose phosphorylase on lipid Langmuir and Langmuir-Blodgett films

Autor Rocha, Jefferson Muniz Autor UNIFESP Google Scholar
Caseli, Luciano Autor UNIFESP Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Resumo The production of bioelectronic devices, including biosensors, can be conducted using enzymes immobilized in ultrathin solid films, for which preserving the enzymatic catalytic activity is crucial for optimal performance. in this sense, nanostructured films that allow for control over molecular architectures are of interest. in this paper, we investigate the adsorption of sucrose phosphorylase onto Langmuir monolayers of the phospholipid dimyristoylphosphatidic acid, which caused the surface pressure isotherms to expand. With polarization-modulated infrared reflection absorption spectroscopy (PM-IRRAS), the amide bands from the enzyme could be identified, with the C-N and C=O dipole moments lying parallel to the air-water interface. Structuring of the enzyme into an alpha-helix was noted, and this structure was preserved when the mixed enzyme-phospholipid monolayer was transferred in the form of a Langmuir-Blodgett (LB) film. the latter was demonstrated with measurements of the catalytic activity of sucrose phosphorylase, which presented the highest enzyme activity for multilayer LB film. the approach presented in this study not only allows for optimized catalytic activity toward sucrose but also permits to explain why certain film architectures exhibit superior performance. (C) 2014 Elsevier B.V. All rights reserved.
Assunto Sucrose phospholysase
Air-water interface
Langmuir monolayers
Enzyme activity
Idioma Inglês
Financiador Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Rede nBioNet: Films and Sensors
Número do financiamento FAPESP: 2013/10213-1
CNPq: 470890/2012-6
Data 2014-04-01
Publicado em Colloids and Surfaces B-biointerfaces. Amsterdam: Elsevier B.V., v. 116, p. 497-501, 2014.
ISSN 0927-7765 (Sherpa/Romeo, fator de impacto)
Editor Elsevier B.V.
Extensão 497-501
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000335706100066

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