Busca avançada
Ano de início
Entree
(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Acylated Carrageenan Changes the Physicochemical Properties of Mixed Enzyme-Lipid Ultrathin Films and Enhances the Catalytic Properties of Sucrose Phosphorylase Nanostructured as Smart Surfaces

Texto completo
Autor(es):
Rocha, Jefferson M. [1] ; Pavinatto, Adriana [2] ; Nobre, Thatyane M. [2] ; Caseli, Luciano [1]
Número total de Autores: 4
Afiliação do(s) autor(es):
[1] Univ Fed Sao Paulo, Inst Environm Chem & Pharmaceut Sci, BR-04021001 Diadema, SP - Brazil
[2] Univ Sao Paulo, Sao Carlos Phys Inst, Rua Sao Nicolau 210, BR-13566590 Sao Carlos, SP - Brazil
Número total de Afiliações: 2
Tipo de documento: Artigo Científico
Fonte: Journal of Physical Chemistry B; v. 120, n. 24, p. 5359-5366, JUN 23 2016.
Citações Web of Science: 8
Resumo

Control over the catalytic activity of enzymes is important to construct biosensors with a wide range of detectability and higher stability. For this, immobilization of enzymes on solid supports as nanostructured films is a current approach that permits easy control of the molecular architecture as well as tuning of the properties. In this article, we employed acylated carrageenan (AC) mixed with phospholipids at the air water interface to facilitate the adsorption of the enzyme sucrose phosphorylase (SP). AC stabilized the adsorption of SP at the phospholipid monolayer, as detected by tensiornetry, by which thermodynamic parameters could be inferred from the surface pressure area isotherm. Also, infrared spectroscopy applied in situ over the monolayer showed that the AC-phospholipid system not only permitted the enzyme to be adsorbed but also helped conserve its secondary structure. The mixed monolayers were then transferred onto solid supports as Langmuir-Blodgett (LB) films and investigated with transfer ratio, quartz crystal microbalance, fluorescence spectroscopy, and atomic force microscopy. The enzyme activity of the LB film was then determined, revealing that although there was an expected reduction in activity in relation to the homogeneous environment the activity could be better preserved after 1 month, revealing enhanced stability. (AU)

Processo FAPESP: 15/23446-0 - Superfícies inteligentes nanoestruturadas e bioinspiradas: investigação de interações em modelos de membrana e produção de dispositivos para biossensores e análise ambiental.
Beneficiário:Luciano Caseli
Modalidade de apoio: Auxílio à Pesquisa - Regular