03 Fakultät Chemie

Permanent URI for this collectionhttps://elib.uni-stuttgart.de/handle/11682/4

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Institute: search.filters.UBSInstitut.Institut für Biomaterialien und biomolekulare SystemeSubject: search.filters.subject.540

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    Piezoelectric templates - new views on biomineralization and biomimetics
    (2016) Stitz, Nina; Eiben, Sabine; Atanasova, Petia; Domingo, Neus; Leineweber, Andreas; Burghard, Zaklina; Bill, Joachim
    Biomineralization in general is based on electrostatic interactions and molecular recognition of organic and inorganic phases. These principles of biomineralization have also been utilized and transferred to bio-inspired synthesis of functional materials during the past decades. Proteins involved in both, biomineralization and bio-inspired processes, are often piezoelectric due to their dipolar character hinting to the impact of a template’s piezoelectricity on mineralization processes. However, the piezoelectric contribution on the mineralization process and especially the interaction of organic and inorganic phases is hardly considered so far. We herein report the successful use of the intrinsic piezoelectric properties of tobacco mosaic virus (TMV) to synthesize piezoelectric ZnO. Such films show a two-fold increase of the piezoelectric coefficient up to 7.2 pm V−1 compared to films synthesized on non-piezoelectric templates. By utilizing the intrinsic piezoelectricity of a biotemplate, we thus established a novel synthesis pathway towards functional materials, which sheds light on the whole field of biomimetics. The obtained results are of even broader and general interest since they are providing a new, more comprehensive insight into the mechanisms involved into biomineralization in living nature.
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    Screening, cloning and biochemical characterisation of novel esterases from bacillus sp. associated with the marine sponge aplysina aerophoba
    (2005) Karpushova, Anna Alexandrovna; Brümmer, Franz; Lange, Stefan; Schmid, Rolf D.
    Two novel esterases (EstB1 and EstB2) were isolated from a genomic library of Bacillus sp. associated with the marine sponge Aplysina aerophoba. EstB1 shows low identity (26-44 %)with the published hydrolases of the genus Bacillus, whereas EstB2 shows high identity (73-74 %) with the carboxylesterases from B. cereus and B. anthracis. Both esterases were efficiently expressed in Escherichia coli under the control of T7 promoter using the vector pET-22b(+). Recombinant EstB1 was purified in a single step to electrophoretic homogeneity by IMAC. A method for the refolding of inclusion bodies formed by the recombinant EstB2 was established to obtain active enzyme. Substrate specificity of the two enzymes towards pnitrophenyl and methyl esters and the respective kinetic parameters Km and Vmax were determined. The temperature optima of EstB1 and EstB2 were determined to be in the range of 30-50°C and 20-35°C, respectively. The pH optima were found to be in the range of 6.5-7.5 and 6.5-8.0, respectively. Both enzymes showed the highest stability in up to 50 % (v/v) DMSO followed by methanol, ethanol and 2-propanol. The influence of high NaCl and KCl concentrations was tested. The inhibition effect of 10-50 mM Zn2+ and 50 mM Mg2+ and Ca2+ ions was observed for both esterases. 1-5 mM PMSF deactivated the enzymes, whereas β-mercaptoethanol, DTT and EDTA had no effect on the enzymes activity.