Microfluidic Reactors Based on Rechargeable Catalytic Porous Supports: Heterogeneous Enzymatic Catalysis via Reversible Host-Guest Interactions
| Autor: | Nelson Vargas-Alfredo, Alexandra Muñoz-Bonilla, Alberto Gallardo, Agatha Bastida, Alberto Sanz de León, Juan Rodríguez-Hernández, Alfonso Fernández-Mayoralas |
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| Přispěvatelé: | Ministerio de Economía y Competitividad (España), Consejo Superior de Investigaciones Científicas (España) |
| Rok vydání: | 2016 |
| Předmět: |
Materials science
Reusable bioreactors 02 engineering and technology 010402 general chemistry 01 natural sciences Horseradish peroxidase Catalysis Styrene Enzyme catalysis Micrometre Enzymatic catalysis chemistry.chemical_compound Surface modification Copolymer Organic chemistry General Materials Science Host−guest interactions Heterogeneous catalysis biology Breath figures technology industry and agriculture Substrate (chemistry) 021001 nanoscience & nanotechnology 0104 chemical sciences chemistry Chemical engineering biology.protein Polystyrene 0210 nano-technology |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname |
| ISSN: | 1944-8252 |
| Popis: | We report on the fabrication of a microfluidic device in which the reservoir contains a porous surface with enzymatic catalytic activity provided by the reversible immobilization of horseradish peroxidase onto micrometer size pores. The porous functional reservoir was obtained by the Breath Figures approach by casting in a moist environment a solution containing a mixture of high molecular weight polystyrene (HPS) and a poly(styrene-co-cyclodextrin based styrene) (P(S-co-SCD)) statistical copolymer. The pores enriched in CD were employed to immobilize horseradish peroxidase (previously modified with adamantane) by hostguest interactions (HRP-Ada). These surfaces exhibit catalytic activity that remains stable during several reaction cycles. Moreover, the porous platforms could be recovered by using free water-soluble β-CD with detergents. An excess of β-CD/TritonX100 in solution disrupts the interactions between HRP-Ada and the CD-modified substrate thus allowing us to recover the employed enzyme and reuse the platform. The authors gratefully acknowledge support from the Consejo Superior de Investigaciones Cientifí cas (CSIC). Equally, this work was financially supported by the Ministerio de Economiá y Competitividad (MINECO) through MAT2013-47902-C2-1-R, MAT2016-78437-R MAT2013-42957-R, MAT2015-65184-C2- 2-R, and CTQ2013-45538-P. |
| Databáze: | OpenAIRE |
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