Production of a recombinant polyester-cleaving hydrolase from Thermobifida fusca in Escherichia coli View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2006-08

AUTHORS

Karolin Dresler, Joop van den Heuvel, Rolf-Joachim Müller, Wolf-Dieter Deckwer

ABSTRACT

The hydrolase (Thermobifida fusca hydrolase; TfH) from T. fusca was produced in Escherichia coli as fusion protein using the OmpA leader sequence and a His(6) tag. Productivity could be raised more than 100-fold. Both batch and fed-batch cultivations yield comparable cell specific productivities whereas volumetric productivities differ largely. In the fed-batch cultivations final rTfH concentrations of 0.5 g L(-1) could be achieved. In batch cultivations the generated rTfH is translocated to the periplasm wherefrom it is completely released into the extracellular medium. In fed-batch runs most of the produced rTfH remains as soluble protein in the cytoplasm and only a fraction of about 35% is translocated to the periplasm. Migration of periplasmic proteins in the medium is obviously coupled with growth rate and this final transport step possibly plays an important role in product localization and efficacy of the Sec translocation process. More... »

PAGES

169-183

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00449-006-0069-9

DOI

http://dx.doi.org/10.1007/s00449-006-0069-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022643110

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16770590


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