ArticleMicrobial biotechnology2020
Improving the autotransporter-based surface display of enzymes in Pseudomonas putida KT2440.
Article in Microbial biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- A plasmid toolbox for the easy autodisplay of recombinant proteins and its optimization.Communications biology · 2026Article
- Engineering a novel carbaryl-degrading esterase from Bacillus velezensis for enhanced degradability via semi-rational design and whole-cell biocatalysis.World journal of microbiology & biotechnology · 2025Article
- Review
- A Novel Thermo-Alkaline Stable GDSL/SGNH Esterase with Broad Substrate Specificity from a Deep-Sea Pseudomonas sp.Marine biotechnology (New York, N.Y.) · 2024Article
- Pseudomonas putida as a platform for medium-chain length α,ω-diol production: Opportunities and challenges.Microbial biotechnology · 2024Article
- Towards synthetic PETtrophy: Engineering Pseudomonas putida for concurrent polyethylene terephthalate (PET) monomer metabolism and PET hydrolase expression.Microbial cell factories · 2022Article
- When metabolic prowess is too much of a good thing: how carbon catabolite repression and metabolic versatility impede production of esterified α,ω-diols in Pseudomonas putida KT2440.Biotechnology for biofuels · 2021Article
- Engineering Tropism ofACS synthetic biology · 2021Article
- Industrial biotechnology of Pseudomonas putida: advances and prospects.Applied microbiology and biotechnology · 2020Review
- Improving the autotransporter-based surface display of enzymes in Pseudomonas putida KT2440.Microbial biotechnology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudomonas putida can be used as a host for the autotransporter-mediated surface display of enzymes (autodisplay), resulting in whole-cell biocatalysts with recombinant functionalities on their cell envelope. The efficiency of autotransporter-mediated secretion depends on the N-terminal signal peptide as well as on the C-terminal translocator domain of autotransporter fusion proteins. We set out to optimize autodisplay for P. putida as the host bacterium by comparing different signal peptides and translocator domains for the surface display of an esterase. The translocator domain did not have a considerable effect on the activity of the whole-cell catalysts. In contrast, by using the signal peptide of the P. putida outer membrane protein OprF, the activity was more than 12-fold enhanced to 638 mU ml
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.