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Pseudomonas as a microbial enzyme factory. The source of industrially potent enzymes and the host for heterologous enzyme production

17 April 2009

PhD ceremony: ms. J.K. Krzeslak, 14.45 uur, Academiegebouw, Broerstraat 5, Groningen

Thesis: Pseudomonas as a microbial enzyme factory. The source of industrially potent enzymes and the host for heterologous enzyme production

Promotor(s): prof. W.J. Quax

Faculty: Mathematics and Natural Sciences

 

The research Joanna Krzeslak presents in her thesis investigates Pseudomonas for the production of pharmaceutically relevant proteins. Pseudomonads can be seen as microbial enzyme factories as they can serve as a potential source of industrially potent enzymes and the host for nanotechnological production of biocatalysts. In particular, the fundamental issues, such as the regulation of the lipase gene expression in P. alcaligenes, secretion of heterologous proteins and a search for industrially potent enzymes within P. aeruginosa, were addressed here. As a result, Krzeslak demonstrated at the molecular level that the LipRQ two-component system of P. alcaligenes governs the regulation of lipase expression by direct LipR binding to the lipase promoter. She also analyzed conditions inducing lipase expression. Furthermore, the observations concerning a putative acylase PA1893 should stimulate future work extended by the list of PA1893 potential substrate compounds to begin with. Finally, a study with P. aeruginosa as a host for heterologous penicillin G acylase (PGA) expression and secretion implied that the periplasmic space of P. aeruginosa can serve as a potent folding compartment for various proteins. Yet, achieving the successful secretion will require further studies before the somewhat universal secretion signal can be defined. Ultimately, the efficient Pseudomonas factory might have to be engineered in a protein-specific manner to fulfill the requirements of a particular heterologous protein.

 

Last modified:15 September 2017 3.39 p.m.

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