Microfluidic Reactors Based on Rechargeable Catalytic Porous Supports: Heterogeneous Enzymatic Catalysis via Reversible Host-Guest Interactions

被引：15

作者：

Sanz de Leon, Alberto ^{[1
,4
]}

Vargas-Alfredo, Nelson ^{[1
]}

Gallardo, Alberto ^{[1
]}

Fernandez-Mayoralas, Alfonso ^{[2
]}

Bastida, Agatha ^{[2
]}

Munoz-Bonilla, Alexandra ^{[1
,3
]}

Rodriguez-Hernandez, Juan ^{[1
]}

机构：

[1] CSIC, Inst Ciencia & Tecnol Polimeros, C Juan Cierva 3, Madrid 28006, Spain

[2] CSIC, IQOG, C Juan Cierva 3, Madrid 28006, Spain

[3] Univ Autonoma Madrid, Fac Ciencias, Dept Quim Fis Aplicada, C Francisco Tomas y Valiente 7, E-28049 Madrid, Spain

[4] Max Planck Inst Colloids & Interfaces, Mechano Bio Chem, Sci Pk Potsdam Golm, D-14424 Potsdam, Germany

来源：

ACS APPLIED MATERIALS & INTERFACES | 2017年 / 9卷 / 04期

关键词：

breath figures; host-guest interactions; enzymatic catalysis; heterogeneous catalysis; reusable bioreactors; surface modification; HONEYCOMB FILMS; IMMOBILIZATION; STABILITY; ENZYMES;

D O I：

10.1021/acsami.6b13554

中图分类号：

TB3 [工程材料学];

学科分类号：

0805 ; 080502 ;

摘要：

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 co-polymer. The pores enriched in CD were employed to immobilize horseradish peroxidase (previously modified with adamantane) by host guest 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 beta-CD with detergents. An excess of beta-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.

引用

页码：4184 / 4191

页数：8