Rapid and simple preparation of thiol-ene emulsion-templated monoliths and their application as enzymatic microreactors

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F15%3A39900260" target="_blank" >RIV/00216275:25310/15:39900260 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68081715:_____/15:00448631

Výsledek na webu

<a href="http://dx.doi.org/10.1039/c5lc00224a" target="_blank" >http://dx.doi.org/10.1039/c5lc00224a</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c5lc00224a" target="_blank" >10.1039/c5lc00224a</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Rapid and simple preparation of thiol-ene emulsion-templated monoliths and their application as enzymatic microreactors

Popis výsledku v původním jazyce

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. Surfacearea 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 viatwo 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

Název v anglickém jazyce

Rapid and simple preparation of thiol-ene emulsion-templated monoliths and their application as enzymatic microreactors

Popis výsledku anglicky

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. Surfacearea 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 viatwo 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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CB - Analytická chemie, separace

OECD FORD obor

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Projekt

<a href="/cs/project/GBP206%2F12%2FG014" target="_blank" >GBP206/12/G014: Centrum pokročilých bioanalytických technologií</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Lab On a Chip

ISSN

1473-0197

e-ISSN

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Svazek periodika

15

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

2162-2172

Kód UT WoS článku

000354196600002

EID výsledku v databázi Scopus

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