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An enzyme-based multi-parameter biosensor is developed for monitoring the concentration of formate, d-lactate, and l-lactate in biological samples. The sensor is based on the specific dehydrogenation by an oxidized β-nicotinamide adenine dinucleotide (NAD+)-dependent dehydrogenase (formate dehydrogenase, d-lactic dehydrogenase, and l-lactic dehydrogenase, respectively) in combination with a diaphorase from Clostridium kluyveri (EC 1.8.1.4). The enzymes are immobilized on a platinum working electrode by cross-linking with glutaraldehyde (GA). The principle of the determination scheme in case of l-lactate is as follows: l-lactic dehydrogenase (l-LDH) converts l-lactate into pyruvate by reaction with NAD+. In the presence of hexacyanoferrate(III), the resulting reduced β-nicotinamide adenine dinucleotide (NADH) is then regenerated enzymatically by diaphorase. The electrochemical detection is based on the current generated by oxidation of hexacyanoferrate(II) at an applied potential of +0.3 V vs. an Ag/AgCl reference electrode. The biosensor will be electrochemically characterized in terms of linear working range and sensitivity. Additionally, the successful practical application of the sensor is demonstrated in an extract from maize silage.
Development and Testing of a Low NOx Micromix Combustion Chamber for an Industrial Gas Turbine
(2015)
Booster stations can fulfill a varying pressure demand with high energy-efficiency, because individual pumps can be deactivated at smaller loads. Although this is a seemingly simple approach, it is not easy to decide precisely when to activate or deactivate pumps. Contemporary activation controls derive the switching points from the current volume flow through the system. However, it is not measured directly for various reasons. Instead, the controller estimates the flow based on other system properties. This causes further uncertainty for the switching decision. In this paper, we present a method to find a robust, yet energy-efficient activation strategy.
Detection of triacetone triperoxide using temperature cycled metal-oxide semiconductor gas sensors
(2015)
An amperometric enzyme biosensor has been applied for the detection of adrenaline. The adrenaline biosensor has been prepared by modification of an oxygen electrode with the enzyme laccase that operates at a broad pH range between pH 3.5 to pH 8. The enzyme molecules were immobilized via cross-linking with glutaraldehyde. The sensitivity of the developed adrenaline biosensor in different pH buffer solutions has been studied.
Laut Zukunftsinstitut (2010) stellt die Individualisierung eine langfristige und nachhaltige Veränderung dar, die die gesamte Gesellschaft (den einzelnen Menschen, Unternehmen, den Staat) betrifft und Auswirkungen auf nahezu alle Lebensbereiche (z. B. Arbeit, Wohnen, Partnerschaft) hat. Die Individualisierung beschreibt dabei die Entwicklung hin zur Fokussierung persönlicher Interessen und Lebensentscheidungen der einzelnen Person (Kunze, Individualisierung, 2011). Der Grund für diese Entwicklung sind laut Kunze (Individualisierung, 2011) Treiber wie steigendes Vermögen, Bildung und Mobilität, was die einzelne Person unabhängiger von größeren Gemeinschaften macht und mehr Freiheit zur Selbstverwirklichung bietet. Als eine Konsequenz daraus werden Wertevorstellungen nicht mehr einfach hingenommen, sondern für die eigene Person überprüft und individualisiert (Kunze, Individualisierung, 2011). So wies Beck bereits 1996 darauf hin, dass Individualisierung meint „erstens die Auflösung und zweitens die Ablösung industriegesellschaftlicher Lebensformen durch andere, in denen die Einzelnen ihre Biographie selbst herstellen, inszenieren, zusammenflickschustern müssen“ (Beck, Die Erfindung des Politischen, 1996, S. 150).