Thiographene synthesized from fluorographene via xanthogenate with immobilized enzymes for environmental remediation

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22310%2F19%3A43918018" target="_blank" >RIV/60461373:22310/19:43918018 - isvavai.cz</a>
Alternative codes found
RIV/00216305:26620/19:PU133202
Result on the web
<a href="https://pubs.rsc.org/en/content/articlepdf/2019/nr/c9nr02376c" target="_blank" >https://pubs.rsc.org/en/content/articlepdf/2019/nr/c9nr02376c</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1039/c9nr02376c" target="_blank" >10.1039/c9nr02376c</a>

Result language
angličtina
Original language name
Thiographene synthesized from fluorographene via xanthogenate with immobilized enzymes for environmental remediation
Original language description
Graphene, graphene oxide and their related thiographene-, hydroxygraphene- or fluorographene-based materials have broad applications. We report on the thiol-functionalization of fluorographene via xanthogenate. Such thiographene contains 5.1 at% of sulphur in the form of thiol groups, which is the highest thiol content reported to date. Such tailored thiographene allows the immobilization of two types of enzymes. Here, we explore the functionalization of highly thiolated graphene with enzymes via physisorption or covalent linkage producing an important heterogeneous biocatalyst platform for wastewater treatment applications. Thiographene modified with a lipase from Mucor miehei can find utilization in lipidrich wastewater treatment whereas the catalase-modified thiographene is intended for bioremediation applications. Upon increasing concentration of the thiol groups on graphene, protein loading of the catalase was increased by 16% and the ester bond cleavage activity of the thiographene-immobilized lipase was 129% that of the free lipase. We expect that such a highly active heterogeneous thiographene-based biocatalyst will find a use in water remediation applications.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10404 - Polymer science

Project
<a href="/en/project/GA17-05421S" target="_blank" >GA17-05421S: New efficient membranes for effective H2 / CO2 separation (HySME)</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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