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为了抵御高温——迄今为止最耐热的丙酮酸脱羧酶的工程改造。

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

作者信息

Sutiono Samuel, Satzinger Katharina, Pick André, Carsten Jörg, Sieber Volker

机构信息

Chair of Chemistry of Biogenic Resources, Campus Straubing for Biotechnology and Sustainability, Technical University of Munich Schulgasse 16 94315 Straubing Germany

Catalytic Research Center, Technical University of Munich Ernst-Otto-Fischer-Straße 1 85748 Garching Germany.

出版信息

RSC Adv. 2019 Sep 20;9(51):29743-29746. doi: 10.1039/c9ra06251c. eCollection 2019 Sep 18.

DOI:10.1039/c9ra06251c
PMID:35531508
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9071941/
Abstract

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.

摘要

丙酮酸脱羧酶（PDC）是高温下乙醇生产和无细胞丁醇合成的关键酶。耐热、有机溶剂稳定的PDC是由细菌PDC进化而来的。新变体在75°C下的半衰期提高了1500倍以上，在50°C下9%（体积）丁醇存在时半衰期增加了5000倍以上。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c267/9071941/a947a32226ac/c9ra06251c-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c267/9071941/c4ab32a8d699/c9ra06251c-s1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c267/9071941/758c76e8a298/c9ra06251c-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c267/9071941/a947a32226ac/c9ra06251c-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c267/9071941/c4ab32a8d699/c9ra06251c-s1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c267/9071941/758c76e8a298/c9ra06251c-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c267/9071941/a947a32226ac/c9ra06251c-f2.jpg

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