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Bacterial lipopolysaccharides (endotoxins) show strong biological effects at very low concentrations in human beings and many animals when entering the blood stream. These include affecting structure and function of organs and cells, changing metabolic functions, raising body temperature, triggering the coagulation cascade, modifying hemodynamics and causing septic shock. Because of this toxicity, the removal of even minute amounts is essential for safe parenteral administration of drugs and also for septic shock patients' care. The absence of a general method for endotoxin removal from liquid interfaces urgently requires finding new methods and materials to overcome this gap. Nanostructured carbonized plant parts is a promising material that showed good adsorption properties due to its vast pore network and high surface area. The aim of this study was comparative measurement of endotoxin- and blood proteins-related adsorption rate and adsorption capacity for different carboneous materials produced at different temperatures and under different surface modifications. As a main surface modificator, positively cbarged polymer, polyethileneimine (PEl) was used. Activated carbon materials showed good adsorption properties for LPS and some proteins used in the experiments. During the batch experiments, several techniques (dust removal, autoclaving) were used and optimized for improving the material's adsorption behavior. Also, with the results obtained it was possible to differentiate the materials according to their adsorption capacity and kinetic characteristics. Modification of the surface apparently has not affected hemoglobin binding to the adsorbent's surface. Obtained adsorption isotherms can be used as a powerful tool for designing of future column-based setups for blood purification from LPS, which is especially important for septic shock treatment.
Gas sensor investigation based on a catalytically activated thin-film thermopile for H2O2 detection
(2010)
Simultaneous detection of cyanide and heavy metals for environmental analysis by means of µISEs
(2010)
Shakedown analysis of two dimensional structures by an edge-based smoothed finite element method
(2010)
Comparison of Intravenous Immunoglobulins for Naturally Occurring Autoantibodies against Amyloid-β
(2010)
A novel scheme for precise diagnostics and effective stabilization of currents in a fuel cell stack
(2010)
Lightning safety guidelines
(2010)
Realization of a calorimetric gas sensor on polyimide foil for applications in aseptic food industry
(2010)
Normative Regulations
(2010)
Hybrid control for autonomous systems — Integrating learning, deliberation and reactive control
(2010)
The determination of spacing, edge and end distance requirements for self-tapping screws requires numerous and comprehensive insertion tests. Yet the results of such tests cannot be transferred to other types of screws or even to screws of different diameter because of differences in shape or geometry. To reduce the effort of insertion tests a new method was developed which allows the estimation of required spacings, distances and timber thickness.
C-terminal truncation of a metagenome-derived detergent protease for effective expression in E. coli
(2010)
Recently, a new alkaline protease named HP70 showing highest homology to extracellular serine proteases of Stenotrophomonas maltophilia and Xanthomonas campestris was found in the course of a metagenome screening for detergent proteases (Niehaus et al., submitted for publication). Attempts to efficiently express the enzyme in common expression hosts had failed. This study reports on the realization of overexpression in Escherichia coli after structural modification of HP70. Modelling of HP70 resulted in a two-domain structure, comprising the catalytic domain and a C-terminal domain which includes about 100 amino acids. On the basis of the modelled structure the enzyme was truncated by deletion of most of the C-terminal domain yielding HP70-C477.
This structural modification allowed effective expression of active enzyme using E. coli BL21-Gold as the host. Specific activity of HP70-C477 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 30 ± 5 U/mg compared to 8 ± 1 U/mg of the native enzyme. HP70-C477 was most active at 40 °C and pH 7–11; these conditions are prerequisite for a potential application as detergent enzyme. Determination of kinetic parameters at 40 °C and pH = 9.5 resulted in KM = 0.23 ± 0.01 mM and kcat = 167.5 ± 3.6 s⁻¹. MS-analysis of peptide fragments obtained from incubation of HP70 and HP70-C477 with insulin B indicated that the C-terminal domain influences the cleavage preferences of the enzyme. Washing experiments confirmed the high potential of HP70-C477 as detergent protease.