Florian Schröper

Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Aachen, North Rhine-Westphalia, Germany

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Publications (8)28.45 Total impact

  • Leonie Davina Fritsch · Stefan Schillberg · Florian Schröper ·
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    ABSTRACT: Reliable techniques to detect the presence and zygosity of transgenic events in plants are crucial for biotechnology research and plant breeding industry. Therefore, we have introduced a novel assay, which enables high-throughput genotyping of transgenic events in maize using duplex real-time PCR. We demonstrated that the presence and zygosity of two selected transgenic events could be detected with high reproducibility and that our method is suitable for rapid genotyping of a large number of samples.
    BioSpektrum 09/2015; 21(5):511-514. DOI:10.1007/s12268-015-0611-x
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    ABSTRACT: Plant pathogens cause major economic losses in the agricultural industry because late detection delays the implementation of measures that can prevent their dissemination. Sensitive and robust procedures for the rapid detection of plant pathogens are therefore required to reduce yield losses and the use of expensive, environmentally-damaging chemicals. Here we describe a simple and portable system for the rapid detection of viral pathogens in infected plants, based on immunofiltration, subsequent magnetic detection and the quantification of magnetically-labeled virus particles. Grapevine fanleaf virus (GFLV) was chosen as a model pathogen. Monoclonal antibodies recognizing the GFLV capsid protein were immobilized onto immunofiltration columns and the same antibodies were linked to magnetic nanoparticles. GFLV was quantified by immunofiltration with magnetic labeling in a double antibody sandwich configuration. A magnetic frequency mixing technique was used for high-sensitivity quantification, in which a two-frequency magnetic excitation field was used to induce a sum-frequency signal in the resonant detection coil, corresponding to the virus concentration within the immunofiltration column. We were able to measure GFLV concentrations in the range 6 ng/mL to 20 μg/mL in less than 30 min. The magnetic immunoassay could also be adapted to detect other plant viruses, including Potato virus X and Tobacco mosaic virus, with detection limits of 2-60 ng/mL. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Applied and Environmental Microbiology 02/2015; 81(9). DOI:10.1128/AEM.03667-14 · 3.67 Impact Factor
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    ABSTRACT: Simple and reliable, high-throughput techniques to detect the zygosity of transgenic events in plants are valuable for biotechnology and plant breeding companies seeking robust genotyping data for the assessment of new lines and the monitoring of breeding programs. We show that next-generation sequencing (NGS) applied to short PCR products spanning the transgene integration site provides accurate zygosity data that are more robust and reliable than those generated by PCR-based methods. The NGS reads covered the 5′ border of the transgenic events (incorporating part of the transgene and the flanking genomic DNA), or the genomic sequences flanking the unfilled transgene integration site at the wild-type locus. We compared the NGS method to competitive real-time PCR with transgene-specific and wild-type-specific primer/probe pairs, one pair matching the 5′ genomic flanking sequence and 5′ part of the transgene and the other matching the unfilled transgene integration site. Although both NGS and real-time PCR provided useful zygosity data, the NGS technique was favorable because it needed fewer optimization steps. It also provided statistically more-reliable evidence for the presence of each allele because each product was often covered by more than 100 reads. The NGS method is also more suitable for the genotyping of large panels of plants because up to 80 million reads can be produced in one sequencing run. Our novel method is therefore ideal for the rapid and accurate genotyping of large numbers of samples.
    Transgenic Research 02/2015; 24(4). DOI:10.1007/s11248-015-9864-x · 2.32 Impact Factor
  • Florian Schröper · Arnd Baumann · Andreas Offenhäusser · Dirk Mayer ·
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    ABSTRACT: During the last decade protein electrochemistry at miniaturized electrodes has become important not only for functional studies of the charge transfer properties of redox proteins but also for fostering the development of sensitive biosensor and bioelectronic devices. One of the major challenges in this field is the directed coupling between electronic and biologically active components. A prerequisite for a fast and reversible electron transfer between electrode and protein is that the protein can be bound to the electrode in a favourable orientation. We examined electrostatic and bioaffinity-tag binding strategies for the directed immobilization of horse heart cytochrome c (cytc) on gold electrode surfaces to achieve this goal. Horse heart cytc was expressed in E. coli either as non-modified or genetically modified, i.e. histidine (his)-tag containing protein. The his-tags were introduced at defined positions at the N- or C-terminus of the polypeptide. It was our aim to generate tagged-versions of cytc that facilitate strong electronic coupling between protein and electrode and, at the same time, retain their catalytic and regulatory properties. The combination of different immobilization strategies, e.g. his-tag and electrostatic immobilization also opens new avenues for bivalent immobilization of proteins. This is of interest for molecular bioelectronic and biosensing applications where the proteins are immobilized between two crossing electrodes.
    Biosensors & Bioelectronics 02/2012; 34(1):171-7. DOI:10.1016/j.bios.2012.01.039 · 6.41 Impact Factor
  • Dong Xiang · Feliks Pyatkov · Florian Schröper · Andreas Offenhäusser · Yi Zhang · Dirk Mayer ·
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    ABSTRACT: A bridged version: Molecular junctions bridged by metal ion complexes were investigated by mechanically controllable break junction experiments on the level of individual molecules. The electrical conductance of the junctions varied strongly with the kind of bonded metal ion, in the order: Ca2+≫Zn2+>Ni2+ (see figure).
    Chemistry - A European Journal 11/2011; 17(47):13166-9. DOI:10.1002/chem.201102915 · 5.73 Impact Factor
  • Florian Schröper · Arnd Baumann · Andreas Offenhäusser · Dirk Mayer ·
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    ABSTRACT: Here, we report a new strategy for the directed bivalent immobilization of cyt c on or between gold electrodes. C-terminal modification with cys- or his-tag did not affect the functional integrity of the protein. In combination with electrostatic protein binding, these tags enable a bifunctional immobilization between two electrodes or alternatively one electrode and interacting enzymes.
    Chemical Communications 08/2010; 46(29):5295-7. DOI:10.1039/c0cc00850h · 6.83 Impact Factor
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    ABSTRACT: Biphasic reaction systems for enzyme catalysis are an elegant way to overcome limited solubility and stability of reactants and facilitate continuous processes. However, many synthetically useful enzymes are not stable in biphasic systems of water and organic solvent. The entrapment in polymer beads of polyvinyl alcohol has been shown to enable the stable operation of enzymes unstable in conventional biphasic reaction systems. We report the extension of this concept to continuous operation in a fluidised bed reactor. The enzyme benzaldehyde lyase was used for the continuous synthesis of enantiopure (R)-3,3'-furoin. The results show enhanced stability with half-life times under operation conditions of more than 100 h, as well as superior enzyme utilisation in terms of productivity. Furthermore, racemisation and oxidation of the product could be successfully prevented under the non-aqueous and inert reaction conditions.
    Biotechnology Journal 05/2006; 1(5):564-8. DOI:10.1002/biot.200600030 · 3.49 Impact Factor
  • Florian Schröper ·

Publication Stats

42 Citations
28.45 Total Impact Points


  • 2012-2015
    • Fraunhofer Institute for Molecular Biology and Applied Ecology IME
      Aachen, North Rhine-Westphalia, Germany
  • 2006
    • RWTH Aachen University
      • Institute for Technical und Macromolecular Chemistry
      Aachen, North Rhine-Westphalia, Germany