To beat the heat – engineering of the most thermostable pyruvate decarboxylase to date

Pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis. Thermostable, organic solvent stable PDC was evolved from bacterial PDCs. The new variant shows >1500-fold-improved half-life at 75 °C and >5000-fold-increased h...

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Detalles Bibliográficos
Autores principales: Sutiono, Samuel, Satzinger, Katharina, Pick, André, Carsten, Jörg, Sieber, Volker
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2019
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9071941/
https://www.ncbi.nlm.nih.gov/pubmed/35531508
http://dx.doi.org/10.1039/c9ra06251c
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author Sutiono, Samuel
Satzinger, Katharina
Pick, André
Carsten, Jörg
Sieber, Volker
author_facet Sutiono, Samuel
Satzinger, Katharina
Pick, André
Carsten, Jörg
Sieber, Volker
author_sort Sutiono, Samuel
collection PubMed
description Pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis. Thermostable, organic solvent stable PDC was evolved from bacterial PDCs. The new variant shows >1500-fold-improved half-life at 75 °C and >5000-fold-increased half-life in the presence of 9 vol% butanol at 50 °C.
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spelling pubmed-90719412022-05-06 To beat the heat – engineering of the most thermostable pyruvate decarboxylase to date Sutiono, Samuel Satzinger, Katharina Pick, André Carsten, Jörg Sieber, Volker RSC Adv Chemistry Pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis. Thermostable, organic solvent stable PDC was evolved from bacterial PDCs. The new variant shows >1500-fold-improved half-life at 75 °C and >5000-fold-increased half-life in the presence of 9 vol% butanol at 50 °C. The Royal Society of Chemistry 2019-09-20 /pmc/articles/PMC9071941/ /pubmed/35531508 http://dx.doi.org/10.1039/c9ra06251c Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Sutiono, Samuel
Satzinger, Katharina
Pick, André
Carsten, Jörg
Sieber, Volker
To beat the heat – engineering of the most thermostable pyruvate decarboxylase to date
title To beat the heat – engineering of the most thermostable pyruvate decarboxylase to date
title_full To beat the heat – engineering of the most thermostable pyruvate decarboxylase to date
title_fullStr To beat the heat – engineering of the most thermostable pyruvate decarboxylase to date
title_full_unstemmed To beat the heat – engineering of the most thermostable pyruvate decarboxylase to date
title_short To beat the heat – engineering of the most thermostable pyruvate decarboxylase to date
title_sort to beat the heat – engineering of the most thermostable pyruvate decarboxylase to date
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9071941/
https://www.ncbi.nlm.nih.gov/pubmed/35531508
http://dx.doi.org/10.1039/c9ra06251c
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