Filmes de Langmuir e Langmuir-Blodgett de lipídios contendo pectinase
In this work, we incorporated the enzyme pectinase into Langmuir monolayers of phospholipid acid dimyristoyl phosphatidic (DMPA) and transferred it to solid supports by the Langmuir-Blodgett (LB) technique. We also combine carbon nanotubes with mixed Langmuir films and investigate their interference...
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| Tipo de recurso: | tesis de maestría |
| Estado: | Versión publicada |
| Fecha de publicación: | 2021 |
| País: | Brasil |
| Institución: | Universidade Federal de São Paulo (UNIFESP) |
| Repositorio: | Repositório Institucional da UNIFESP |
| Idioma: | portugués |
| OAI Identifier: | oai:repositorio.unifesp.br:11600/68090 |
| Acceso en línea: | https://sucupira.capes.gov.br/sucupira/public/consultas/coleta/trabalhoConclusao/viewTrabalhoConclusao.jsf?popup=true&id_trabalho=10432292 https://repositorio.unifesp.br/handle/11600/68090 |
| Access Level: | acceso abierto |
| Palabra clave: | Langmuir-Blodgett Langmuir Pectinase Carbon Nanotubes Enzima Nanotubos De Carbono |
| Sumario: | In this work, we incorporated the enzyme pectinase into Langmuir monolayers of phospholipid acid dimyristoyl phosphatidic (DMPA) and transferred it to solid supports by the Langmuir-Blodgett (LB) technique. We also combine carbon nanotubes with mixed Langmuir films and investigate their interference with the physicochemical properties of ultrafine films. The enzyme of choice in this work is easily produced from filamentous fungi type A. niger. DMPA was chosen because it is an anionic lipid that can have interesting interactions with the enzyme in the study pH range and carbon nanotubes were used because they are known in the literature as enhancers of the analytical signal and the preservation of the enzymatic structure. The supramolecular structure of the Langmuir monolayer was stabilized by the incorporation of the enzyme from the formation of metastable structures. The presence of carbon nanotubes gave the films an enzyme activity superior to that of the enzyme incorporated into the DMPA monolayers. The results presented here show an alternative in the perspective of the development of new bioinspired films for biosensing applications aimed at analytical purposes. |
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