Improving the autotransporter-based surface display of enzymes in Pseudomonas putida KT2440.

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 t

SUBMITTER: Tozakidis IEP 

PROVIDER: S-EPMC6922575 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature