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Rapid and simple preparation of thiol–ene emulsion-templated monoliths and their application as enzymatic microreactors
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SYSNO ASEP 0448631 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Rapid and simple preparation of thiol–ene emulsion-templated monoliths and their application as enzymatic microreactors Author(s) Lafleur, J. P. (DK)
Senkbeil, S. (DK)
Novotný, Jakub (UIACH-O) ORCID
Nys, G. (BE)
Bøgelund, N. (DK)
Rand, K. D. (DK)
Foret, František (UIACH-O) RID, ORCID
Kutter, J. P. (DK)Number of authors 8 Source Title Lab on a Chip. - : Royal Society of Chemistry - ISSN 1473-0197
Roč. 15, č. 10 (2015), s. 2162-2172Number of pages 11 s. Publication form Print - P Language eng - English Country GB - United Kingdom Keywords thiol-enes ; mictoreactor ; monolith ; fabrication ; proteins Subject RIV CB - Analytical Chemistry, Separation R&D Projects GBP206/12/G014 GA ČR - Czech Science Foundation (CSF) Institutional support UIACH-O - RVO:68081715 UT WOS 000354196600002 DOI 10.1039/c5lc00224a Annotation A novel, rapid and simple method for the preparation of emulsion-templated monoliths in microfluidic channels based on thiol-ene chemistry is presented. The method allows monolith synthesis and anchoring inside thiol-ene microchannels in a single photoinitiated step. Characterization by scanning electron microscopy showed that the methanol-based emulsion templating process resulted in a network of highly interconnected and regular thiol-ene beads anchored solidly inside thiol-ene microchannels. Surface area measurements indicate that the monoliths are macroporous, with no or little micro- or mesopores. As a demonstration, galactose oxidase and peptide-N-glycosidase F (PNGase F) were immobilized at the surface of the synthesized thiol-ene monoliths via two different mechanisms. First, cysteine groups on the protein surface were used for reversible covalent linkage to free thiol functional groups on the monoliths. Second, covalent linkage was achieved via free primary amino groups on the protein surface by means of thiol-ene click chemistry and L-ascorbic acid linkage. Thus prepared galactose oxidase and PNGase F microreactors demonstrated good enzymatic activity in a galactose assay and the deglycosilation of ribonuclease B, respectively. Workplace Institute of Analytical Chemistry Contact Iveta Drobníková, drobnikova@iach.cz, Tel.: 532 290 234 Year of Publishing 2016
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