An alginate-confined peroxygenase-CLEA for styrene epoxidation

Oxyfunctionalisation reactions in neat substrate still pose a challenge for biocatalysis. Here, we report an alginate-confined peroxygenase-CLEA to catalyse the enantioselective epoxidation of cis-β-methylstyrene in a solvent-free reaction system achieving turnover numbers of 96 000 for the biocatal...

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Detalles Bibliográficos
Autores principales: Nintzel, Friederike E. H., Wu, Yinqi, Planchestainer, Matteo, Held, Martin, Alcalde, Miguel, Hollmann, Frank
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2021
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8191455/
https://www.ncbi.nlm.nih.gov/pubmed/33987632
http://dx.doi.org/10.1039/d1cc01868j
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author Nintzel, Friederike E. H.
Wu, Yinqi
Planchestainer, Matteo
Held, Martin
Alcalde, Miguel
Hollmann, Frank
author_facet Nintzel, Friederike E. H.
Wu, Yinqi
Planchestainer, Matteo
Held, Martin
Alcalde, Miguel
Hollmann, Frank
author_sort Nintzel, Friederike E. H.
collection PubMed
description Oxyfunctionalisation reactions in neat substrate still pose a challenge for biocatalysis. Here, we report an alginate-confined peroxygenase-CLEA to catalyse the enantioselective epoxidation of cis-β-methylstyrene in a solvent-free reaction system achieving turnover numbers of 96 000 for the biocatalyst and epoxide concentrations of 48 mM.
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spelling pubmed-81914552021-06-29 An alginate-confined peroxygenase-CLEA for styrene epoxidation Nintzel, Friederike E. H. Wu, Yinqi Planchestainer, Matteo Held, Martin Alcalde, Miguel Hollmann, Frank Chem Commun (Camb) Chemistry Oxyfunctionalisation reactions in neat substrate still pose a challenge for biocatalysis. Here, we report an alginate-confined peroxygenase-CLEA to catalyse the enantioselective epoxidation of cis-β-methylstyrene in a solvent-free reaction system achieving turnover numbers of 96 000 for the biocatalyst and epoxide concentrations of 48 mM. The Royal Society of Chemistry 2021-05-07 /pmc/articles/PMC8191455/ /pubmed/33987632 http://dx.doi.org/10.1039/d1cc01868j Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Nintzel, Friederike E. H.
Wu, Yinqi
Planchestainer, Matteo
Held, Martin
Alcalde, Miguel
Hollmann, Frank
An alginate-confined peroxygenase-CLEA for styrene epoxidation
title An alginate-confined peroxygenase-CLEA for styrene epoxidation
title_full An alginate-confined peroxygenase-CLEA for styrene epoxidation
title_fullStr An alginate-confined peroxygenase-CLEA for styrene epoxidation
title_full_unstemmed An alginate-confined peroxygenase-CLEA for styrene epoxidation
title_short An alginate-confined peroxygenase-CLEA for styrene epoxidation
title_sort alginate-confined peroxygenase-clea for styrene epoxidation
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8191455/
https://www.ncbi.nlm.nih.gov/pubmed/33987632
http://dx.doi.org/10.1039/d1cc01868j
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