Junior Research Group FOOD-NMR

We are a junior research group in the field of bioorganic-analytical chemistry with a focus on NMR spectroscopy. Applications include the authenticity control of food (metabolomics) as well as NMR spectroscopic analyzes of biochemical reactions (enzyme kinetics) and the interaction of bioorganic molecules with their receptor (STD NMR). The junior research group is located at the HAMBURG SCHOOL OF FOOD SCIENCE and the INSTITUTE OF CHEMISTRY at the University of Hamburg.

Research interests are:

Authenticity control

The geographic origin influences the composition of the metabolic products (metabolites), e.g. due to different exogenous factors (such as soil, temperature, water availability or fertilization). The detection of the metabolites by means of NMR spectroscopy (Nuclear Magnetic Resonance) provides a kind of molecular fingerprint which can be analyzed using statistical methods, e.g. with regard to the question of geographical origin.

Such metabolic analyzes allow the identification of a large number of metabolites in a single measurement without the selection of specific analytes (non-targeted analysis). An NMR spectrum can contain signals for up to 200 metabolites. The identification of specific chemical markers for origin differentiation from complex mixtures represents a further challenge. We elaborate strategies that simplify identification without having to isolate single compounds in a time-consuming manner (targeted analysis). For this purpose, we apply various methods such as high-performance liquid chromatography and mass spectrometry in combination with NMR spectroscopy, using the complementarity of the respective methods.

Enzyme kinetics

Enzyme kinetics has the goal of the functional characterization of enzymes, as well as their inhibitors and activators. In accordance with the diversity of the enzymes catalyzed by enzymes, a broad range of methods can be used, with which kinetic analyzes can be carried out. NMR spectroscopy is rarely used, although direct quantification is carried out without a modification of the substrates and the course of the reaction can be followed in atomic resolution.

STD NMR (saturation transfer difference NMR)

Application of STD NMR for the analysis of protein-ligand interactions. This may, for example, be the interaction of a substrate with its enzyme or a potential agent with a receptor.


References to specific research topics:

Detection of a Toxic Methylated Derivative of Phomopsin A Produced by the Legume-Infesting Fungus Diaporthetoxica
Schloß, T. Hackl, C. Herz, E. Lamy, M. Koch, S. Rohn, R. Maul
Journal of Natural Products 80, 1930–1934 (2017)

Food Fingerprinting: Metabolomic approaches for geographical origin discrimination of hazelnuts (Corylus avellana) by UPLC-QTOF-MS
Klockmann, E.Reiner, R. Bachmann, T. Hackl, M. Fischer
Journal of Agricultural and Food Chemistry 64, 9253-9262 (2016)

Synthesis and Evaluation of Neoglycoconjugates Based on Adamantyl Scaffolds
Fleck, E. Memmel, M. Fölsing, B. Poll, T. Hackl, J. Seibel, W. Maison
European Journal of Organic Chemistry 1696-1710 (2015)

A Non-Ionic Inhibitor with High Specificity for the UDP-Gal Donor Binding Site of Human Blood Group B Galactosyltransferase – Design, Synthesis and Characterization
Schaefer, N. Sindhuwinata, T. Hackl, M. P. Koetzler, F. C. Niemeyer, M. M. Palcic, T. Peters, B. Meyer
Journal of Medicinal Chemistry 56, 2150-2154 (2013)

NMR for direct determination of Km and Vmax of enzyme reactions based on the Lambert W function-analysis of progress curves
F. Exnowitz, B. Meyer, T. Hackl
Biochimica et Biophysica Acta, Proteins and Proteomics 1824, 443-449 (2012)

Isogermacrene A, a proposed intermediate in sesquiterpene biosynthesis
T. Hackl, W. A. König, H. Muhle
Phytochemistry 65, 2261-2275 (2004)


University of Hamburg
Department of Chemistry
Martin-Luther-King-Platz 6
20146 Hamburg

Tel.: +49 40 42838 2831