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Puorger, C.

Publications and source records attributed to Puorger, C..

2 recordsLinked to original sources

Compost bacteria as a promising new solution for degradation of diclofenac and related pharmaceuticals for water treatment processes

Diclofenac, a widely used pharmaceutical, poses a significant environmental problem due to its persistence in aquatic systems and resistance to conventional degradation processes. Mesophilic microorganisms, commonly employed in wastewater treatment, often struggle to break down diclofenac, necessitating alternative approaches for its removal. In this study, we investigated thermophilic compost microorganisms and their ability to degrade diclofenac. Compost communities were cultivated for 20 weeks at 50{degrees}C in a membrane bioreactor, with a continuous supply of 2 mg/L diclofenac as the sole carbon source. After two weeks, the microbial community steadily enhanced its ability to remove diclofenac, achieving removal rates up to 60%. The consortium demonstrated flexibility in the degradation of further pollutants, namely sulfamethoxazole, paracetamol, and ciprofloxacin, with changes in their community structure depending on the substrates. In addition, thermophilic isolates Chelatococcus sp. strain D3 and Mycobacterium sp. strain D1 were characterized and demonstrated variation in the first reaction of transforming diclofenac, which is the crucial step in mineralization of this pollutant, resulting in either 4-hydroxy-diclofenac or diclofenac-lactam, respectively. Furthermore, Chelotococcus sp. strain D3 demonstrated the capability to catalyze the biotransformation of diclofenac into 4-hydroxydiclofenac in treated wastewater. Notably, this transformation was effectively carried out even at lower temperatures (25 {degrees}C and 37{degrees}C). These results show that the use of thermophilic consortia can be applied for efficient bioremediation in wastewater treatment plants, specifically for compounds that mesophilic organisms degrade poorly.

microbiology↗

Stochastic chain termination in bacterial pilus assembly

Adhesive type 1 pili from uropathogenic Escherichia coli strains are filamentous, supramolecular protein complexes consisting of a short tip fibrillum and a long, helical rod formed by up to several thousand copies of the major pilus subunit FimA. Here, we reconstituted the entire type 1 pilus rod assembly reaction in vitro, using all constituent protein subunits in the presence of the assembly platform FimD, and identified the so-far uncharacterized subunit FimI as an irreversible assembly terminator. We provide a complete, quantitative model of pilus rod assembly kinetics based on the measured rate constants of FimD-catalyzed subunit incorporation. The model reliably predicts the length distribution of assembled pilus rods as a function of the ratio between FimI and the main pilus subunit FimA and is fully consistent with the length distribution of membrane-anchored pili assembled in vivo. The results show that the natural length distribution of adhesive pili formed via the chaperone-usher pathway results from a stochastic chain termination reaction.

biophysics↗