Erythromycin degradation by an esterase in enzymatic membrane reactors

1 Introduction Pharmaceuticals products (PPs) and endocrine disrupting chemicals (EDCs) as well as their transformation products have been detected in almost all effluents from sewage facilities, in surface water, in groundwater, adsorbed on sediments and even in drinking water [1,2]. Ecotoxicity studies have demonstrated that pharmaceutical pollutants could affect the growth, reproduction and behavior of birds, fishes, invertebrates, plants and bacteria [3,4]. Some recently published studies report that the presence of low concentrations of antibiotics in the wastewaters may develop antibiotic resistance in the whole environment [5, 6]. As previously reported by Demarche et al. [7], the use of enzymes might be beneficial to enhance or complement conventional wastewater treatments. As far as enzymes are relatively expensive the reuse of the biocatalyst appears to be essential to ensure the economic and industrial viability of the process. Enzymatic membrane reactors appear to be an interesting alternative since they enable to couple reaction and separation [8]. In fact, in such enzymatic reactors, the substrate is continuously brought in contact with the biocatalyst, which is retained by the membrane, either freely circulating with the retentate or fixed on or within the membrane and the reaction products are recovered in the permeate. This work describes the study of erythromycin degradation by an EreB esterase in free and immobilized forms. It focuses on the comparison between 3 different enzymatic membrane reactors for erythromycin degradation by esterase EreB. In the first configuration the free biocatalyst was confined in the reaction media by a ceramic membrane. In the two other cases, the enzyme was immobilized in the membrane either covalently grafted or adsorbed. Please click Additional Files below to see the full abstract

DNA condensation by TmHU studied by optical tweezers, AFM and molecular dynamics simulations

The compaction of DNA by the HU protein from Thermotoga maritima (TmHU) is analysed on a single-molecule level by the usage of an optical tweezers-assisted force clamp. The condensation reaction is investigated at forces between 2 and 40 pN applied to the ends of the DNA as well as in dependence on the TmHU concentration. At 2 and 5 pN, the DNA compaction down to 30% of the initial end-to-end distance takes place in two regimes. Increasing the force changes the progression of the reaction until almost nothing is observed at 40 pN. Based on the results of steered molecular dynamics simulations, the first regime of the length reduction is assigned to a primary level of DNA compaction by TmHU. The second one is supposed to correspond to the formation of higher levels of structural organisation. These findings are supported by results obtained by atomic force microscopy