Ectoine Production Using Novel Heterologous EctABC<i><sub>S. salarius</sub></i> from Marine Bacterium <i>Salinicola salarius</i>
Ectoine, a heterocyclic amino acid produced by various bacteria, was widely used in the fields of cosmetics and medicine. In this study, a novel ectoine synthesis cluster from marine bacterium <i>Salinicola salarius</i> 1A01339 was firstly introduced into <i>Escherichia coli</i&...
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doaj-0d7683e0cd89465080c02119112c878e2021-08-06T15:18:59ZengMDPI AGApplied Sciences2076-34172021-07-01116873687310.3390/app11156873Ectoine Production Using Novel Heterologous EctABC<i><sub>S. salarius</sub></i> from Marine Bacterium <i>Salinicola salarius</i>Yue Su0Wenting Peng1Tong Wang2Yanhui Li3Luyu Zhao4Xinyu Wang5Ying Li6Ling Lin7Anhui Provincial Key Laboratory of Molecular Enzymology and Mechanism of Major Diseases, 1 Beijing East Road, Wuhu 241000, ChinaAnhui Provincial Key Laboratory of Molecular Enzymology and Mechanism of Major Diseases, 1 Beijing East Road, Wuhu 241000, ChinaAnhui Provincial Key Laboratory of Molecular Enzymology and Mechanism of Major Diseases, 1 Beijing East Road, Wuhu 241000, ChinaAnhui Provincial Key Laboratory of Molecular Enzymology and Mechanism of Major Diseases, 1 Beijing East Road, Wuhu 241000, ChinaAnhui Provincial Key Laboratory of Molecular Enzymology and Mechanism of Major Diseases, 1 Beijing East Road, Wuhu 241000, ChinaAnhui Provincial Key Laboratory of Molecular Enzymology and Mechanism of Major Diseases, 1 Beijing East Road, Wuhu 241000, ChinaAnhui Provincial Key Laboratory of Molecular Enzymology and Mechanism of Major Diseases, 1 Beijing East Road, Wuhu 241000, ChinaAnhui Provincial Key Laboratory of Molecular Enzymology and Mechanism of Major Diseases, 1 Beijing East Road, Wuhu 241000, ChinaEctoine, a heterocyclic amino acid produced by various bacteria, was widely used in the fields of cosmetics and medicine. In this study, a novel ectoine synthesis cluster from marine bacterium <i>Salinicola salarius</i> 1A01339 was firstly introduced into <i>Escherichia coli</i> BL21(DE3) for heterologous production of ectoine. The bioinformatic analysis proved the function of these ectoine synthesis enzymes, and showed the highest identities of 83.3–87.7% with enzymes from other microorganisms. Using the whole-cell biocatalytic method, 3.28 g/L ectoine was synthesized and excreted into the medium with the substrate of 200 mM sodium aspartate at 25 °C, pH 6.5 in flask-level. Further bioconversion was performed in the fermentor system at the high cell density of 20 OD/mL, and the concentration of extracellular ectoine was increased to 22.5 g/L in 24 h (equivalent to the specific productivity of 0.94 g/L·h), achieving over 6 times of production compared with that in flasks. Significantly, the recombinant strain demonstrated a lower catalytic temperature with the optimum of 25 °C, and a stronger tolerance to the substrate aspartate of 300 mM. These results might provide a compelling case for ectoine synthesis as well as potential applications in large-scale industrial production.https://www.mdpi.com/2076-3417/11/15/6873ectoine<i>Salinicola salarius</i>marine bacteriawhole-cell biocatalysis |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yue Su Wenting Peng Tong Wang Yanhui Li Luyu Zhao Xinyu Wang Ying Li Ling Lin |
spellingShingle |
Yue Su Wenting Peng Tong Wang Yanhui Li Luyu Zhao Xinyu Wang Ying Li Ling Lin Ectoine Production Using Novel Heterologous EctABC<i><sub>S. salarius</sub></i> from Marine Bacterium <i>Salinicola salarius</i> Applied Sciences ectoine <i>Salinicola salarius</i> marine bacteria whole-cell biocatalysis |
author_facet |
Yue Su Wenting Peng Tong Wang Yanhui Li Luyu Zhao Xinyu Wang Ying Li Ling Lin |
author_sort |
Yue Su |
title |
Ectoine Production Using Novel Heterologous EctABC<i><sub>S. salarius</sub></i> from Marine Bacterium <i>Salinicola salarius</i> |
title_short |
Ectoine Production Using Novel Heterologous EctABC<i><sub>S. salarius</sub></i> from Marine Bacterium <i>Salinicola salarius</i> |
title_full |
Ectoine Production Using Novel Heterologous EctABC<i><sub>S. salarius</sub></i> from Marine Bacterium <i>Salinicola salarius</i> |
title_fullStr |
Ectoine Production Using Novel Heterologous EctABC<i><sub>S. salarius</sub></i> from Marine Bacterium <i>Salinicola salarius</i> |
title_full_unstemmed |
Ectoine Production Using Novel Heterologous EctABC<i><sub>S. salarius</sub></i> from Marine Bacterium <i>Salinicola salarius</i> |
title_sort |
ectoine production using novel heterologous ectabc<i><sub>s. salarius</sub></i> from marine bacterium <i>salinicola salarius</i> |
publisher |
MDPI AG |
series |
Applied Sciences |
issn |
2076-3417 |
publishDate |
2021-07-01 |
description |
Ectoine, a heterocyclic amino acid produced by various bacteria, was widely used in the fields of cosmetics and medicine. In this study, a novel ectoine synthesis cluster from marine bacterium <i>Salinicola salarius</i> 1A01339 was firstly introduced into <i>Escherichia coli</i> BL21(DE3) for heterologous production of ectoine. The bioinformatic analysis proved the function of these ectoine synthesis enzymes, and showed the highest identities of 83.3–87.7% with enzymes from other microorganisms. Using the whole-cell biocatalytic method, 3.28 g/L ectoine was synthesized and excreted into the medium with the substrate of 200 mM sodium aspartate at 25 °C, pH 6.5 in flask-level. Further bioconversion was performed in the fermentor system at the high cell density of 20 OD/mL, and the concentration of extracellular ectoine was increased to 22.5 g/L in 24 h (equivalent to the specific productivity of 0.94 g/L·h), achieving over 6 times of production compared with that in flasks. Significantly, the recombinant strain demonstrated a lower catalytic temperature with the optimum of 25 °C, and a stronger tolerance to the substrate aspartate of 300 mM. These results might provide a compelling case for ectoine synthesis as well as potential applications in large-scale industrial production. |
topic |
ectoine <i>Salinicola salarius</i> marine bacteria whole-cell biocatalysis |
url |
https://www.mdpi.com/2076-3417/11/15/6873 |
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