English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Phenazine-1-carboxylic acid (PCA) and its derivative pyocyanin (PYO) are natural redox mediators in bioelectrochemical systems and have the potential to enable new bioelectrochemical production strategies. The native producer  Pseudomonas aeruginosa  harbors two identically structured operons in its genome, which encode the enzymes responsible for PCA synthesis [ phzA1-G1  (operon 1),  phzA2-G2  (operon 2)]. To optimize heterologous phenazines production in the biotech host  Pseudomonas putida  KT2440, we compared PCA production from both operons originating from  P. aeruginosa  strain PAO1 ( O1.phz1  and  O1.phz2 ) as well as from  P. aeruginosa  strain PA14 ( 14.phz1  and  14.phz2 ). Comparisons of phenazine synthesis and bioelectrochemical activity were performed between heterologous constructs with and without the combination with the genes  phzM  and  phzS  required to convert PCA to PYO. Despite a high amino acid homology of all enzymes of more than 97%,  P. putida  harboring  14.phz2  produced 4-times higher PCA concentrations (80 μg/mL), which resulted in 3-times higher current densities (12 μA/cm 2 ) compared to  P. putida  14.phz1. The respective PCA/PYO producer containing the  14.phz2  operon was the best strain with 80 μg/mL PCA, 11 μg/mL PYO, and 22 μA/cm 2  current density. Tailoring phenazine production also resulted in improved oxygen-limited metabolic activity of the bacterium through enhanced anodic electron discharge. To elucidate the reason for this superior performance, a detailed structure comparison of the PCA-synthesizing proteins has been performed. The here presented characterization and optimization of these new strains will be useful to improve electroactivity in  P. putida  for oxygen-limited biocatalysis.

Boosting Heterologous Phenazine Production in Pseudomonas putida KT2440 Through the Exploration of the Natural Sequence Space