Research field Prof. Dr. Georg Sprenger

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Research field

We are investigating enzymes that can make or cleave C-C bonds, as these are suitable biocatalysts in chemo-enzymatic syntheses, e.g. to produce novel hydroxylated compounds. We are also working on the targeted modification of the metabolic pathways of E. coli and Corynebacterium glutamicum for the production of aromatic compounds, e.g. amino acids such as phenylalanine or tryptophan, violacein and other fine chemicals.

Among the aldolases, we investigated the transaldolase (TAL) and the structurally related, novel fructose-6-phosphate aldolase (FSA) and their mutant proteins (muteins). In cooperation with Prof. Gunter Schneider at the Karolinska Institute in Stockholm, the three-dimensional structures of TAL and some TAL muteins were solved. For the first time, the enzyme:substrate complex of the Schiff base type was elucidated for aldolases. The structure of the decameric enzyme FSA was also solved. The active centres of the enzymes were changed by site-directed mutagenesis and these "muteins" were then investigated for their catalytic properties. In collaboration with Prof. W.D. Fessner's group at the TU Darmstadt, the directed evolution of transaldolase to obtain new enzyme properties was successfully investigated. Mutant proteins with novel or improved properties could be obtained (e.g. dihydroxyacetone as donor substrate for TAL reactions; unphosphorylated aldehydes as acceptor substrate). We thus have various TAL and FSA mutant proteins that provide access to interesting new sugars and sugar analogues from chemo-enzymatic syntheses. We have been able to demonstrate this in collaboration with various research groups (Fessner, Lemaire, Clapés). A DFG project (Dr. Anne Samland) dealt with the determinants of substrate and stereoselectivity of dihydroxyacetone utilising transaldolases and FSA. A variant of FSA with the amino acid substitution Ala129>Ser (A129S) shows significantly improved catalytic efficiency towards fructose-6-phosphate. We recently successfully used this property to redirect glycolysis in an E. coli mutant lacking the functions of phosphofructokinase and glucose-6-phosphate dehydrogenase.

Various thiamine diphosphate (ThDP)-dependent enzymes can - apart from their functions in metabolism - also be used as biocatalysts for C-C bond linkages. In the past, we investigated transketolase (TKT), the structurally related 1-deoxyxylulose 5-phosphate synthase (DXS) from E. coli and phosphonopyruvate decarboxylase (PPDC, from Streptomyces viridochromogenes).

Within the framework of a DFG research group (For 1296), we investigated the use of the enzyme MenD (SEPHCHC synthase) as a novel biocatalyst for 1,2- and 1,4-additions in cooperation with the group of Jürgen Pleiss (ITB, Univ. Stuttgart) and Michael Müller (Univ. Freiburg). Here, too, mutant proteins were generated and - in cooperation with Prof. Gunter Schneider - investigated for their structure-function relationships. In addition to its actual donor 2-ketoglutarate, MenD also uses 2-keto-4-hydroxyglutarate; this opens up new synthesis possibilities.

Using E.coli cells as an example, it was shown that the aromatic biosynthesis pathway (shikimic acid pathway) in bacteria could be successfully optimised for the production of aromatic amino acids such as L-phenylalanine, L-tryptophan, p-aminophenylalanine and phenylglycine. Likewise, other chorismate-derived substances such as violacein (via the intermediate L-tryptophan) could be obtained. Further investigations concern the extraction of aromatic substances with the bacterium Corynebacterium glutamicum; here there is a long-standing cooperation with Covestro AG (formerly Bayer Material Sciences) within the framework of a project supported by the FNR (Bio4PurPro) for the extraction of BioAniline from renewable plant raw materials. In the case of both E. coli and C. glutamicum, it was shown that the targeted chromosomal integration of genes (partly in higher gene copy numbers) has advantages over plasmid-based expression.

In a joint BMBF project (ReCOgNice) with partners from Stuttgart (Prof. Takors, Prof. Sawodny) and from the University of Tübingen (Dr. Bonin), we investigated regulatory processes of the C, O and N metabolic pathways of E. coli cells and were able to construct a large number of defined E. coli strains as reporters for different stress states. In long-term DFG projects (together with Prof. D. Weuster-Botz, TU Munich) we first investigated the production of L-phenylalanine based on glycerol with E. coli. In a recently completed continuation project, strains producing L-tryptophan were investigated. The aim was to elucidate the metabolic adaptation after the change of growth medium (short-term fermentations) and with e.g. supplementary feeding of shikimate. In cooperation with Prof. C. Wittmann (Saarland University) we had successfully used E. coli tryptophan producers for the production of deoxy-violacein. This work is currently being continued within the framework of the DFG priority project (InterZell, SPP2170, in cooperation with IBVT, Prof. Ralf Takors) with the aim of obtaining violacein using bacterial co-cultures (MiMiCry). Through targeted genetic intervention in the central metabolism of E. coli cells (interruption of the function of phosphofructokinase) and by expressing a variant of fructose-6-phosphate aldolase (FSA, Ala129Ser mutant), we were recently able to obtain an E. coli strain that exhibits a novel metabolic pathway to dihydroxyacetone and glycerol.

In a project of the Baden-Württemberg Foundation (BWS; Glycomics/Glycobiology), we first investigated the biotechnological production of fucosylated oligosaccharides ("human milk oligosaccharides, HMO) using recombinant E. coli strains. We were able to produce e.g. 2'-fucosyllactose and fucosylated lacto-N-tetraose. In another (recently completed BWS project), we investigated the formation of non-proteinogenic amino acids such as phenylglycine as building blocks for the production of derivatives of the glycopeptide antibiotics balhimycin or pristinamycin together with partners at the University of Tübingen and the Leibniz Centre/TU Braunschweig.


(If authors from different institutes contributed to the paper, the IMB's co-authors are highlighted in bold)

Jia, J., Huang, W., Schörken, U., Sahm, H., Sprenger, G.A., Lindqvist, Y., & G. Schneider (1996). Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the a/b-barrel within the class I aldolase family. Structure 4:715-724.

Jia, J., Schörken, U., Lindqvist, Y., Sprenger, G.A., & Schneider, G. (1997) Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases. Protein Science 6: 119-124.

Sprenger, G.A., Schörken, U., Wiegert, T., Grolle, S., de Graaf, A.A., Taylor, S.V., Begley, T.P., Bringer-Meyer, S., & Sahm, H. (1997) Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol. Proceedings of the National Academy of Sciences, U.S.A. 94:12857-12862.

Taylor, S.V., Vu, L.D., Begley, T.P., Schörken, U., Grolle, S., Sprenger, G.A., Bringer-Meyer, S., & Sahm, H. (1998) Chemical and enzymatic synthesis of 1-deoxy-D-xylulose-5-phosphate. Journal of Organic Chemistry 63:2375-2377.

Zimmermann, F.T., Schneider, A., Schörken, U., Sprenger, G.A., & Fessner, W-D. (1999) Efficient multi-enzymatic synthesis of D-xylulose 5-phosphate. Tetrahedron Asymmetry 10: 1643-1646.

Schürmann, Me., & Sprenger, G.A. (2001) Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases. Journal of Biological Chemistry, 276:11055-11061.

Schörken, U., Thorell, S., Schürmann, M., Jia, J., Sprenger, G.A., & Schneider, G. (2001) Identification of catalytically important residues in the active site of Escherichia coli transaldolase. European Journal of Biochemistry, 268:2408-2415.

Jossek, R., Bongaerts, J., & Sprenger, G.A. (2001) Characterization of a new feedback-resistant 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Escherichia coli. FEMS Microbiology Letters, 202: 145-148.

Thorell, S., Schürmann, M., Sprenger, G.A., & Schneider, G. (2002) Crystal structure of decameric fructose-6-phosphate aldolase from Escherichia coli reveals inter-subunit helix swapping as a structural basis for assembly differences in the transaldolase family. Journal of Molecular Biology, 319:161-171.

Schürmann, M., Schürmann, M., & Sprenger, G.A. (2002) Fructose 6-phosphate aldolase and 1-deoxy-D-xylulose 5-phosphate synthase from Escherichia coli as tools in enzymatic synthesis of 1-deoxy sugars. Journal of Molecular Catalysis B: Enzymatic, 19-20: 247-252.

Gonzalez-Garcia, E., Helaine, V., Klein, G., Schuermann, M., Sprenger, G.A., Fessner W-D., & Reymond, J-L. (2003) Fluorogenic stereochemical probes for transaldolases. Chemistry, a European Journal, 9: 893-899.

Vasic-Racki, D., Bongs J., Schörken, U., Sprenger, G.A., & Liese, A. (2003) Modeling of reaction kinetics for reactor selection in the case of L-erythrulose synthesis. Bioprocess Engineering, 25: 285-290.

Pohl, M., Sprenger, G.A., & Müller, M. (2004) A new perspective on thiamine catalysis. Current Opinion in Biotechnology, 15: 335-342.

Samland AK, Sprenger GA (2006) Microbial aldolases as C-C bonding enzymes – unknown treasures and new developments. Applied Microbiology and Biotechnology, 71: 253-264.

Castillo, J.A., Calveras, J., Casas, J., Mitjans, M., Vinardell, P., Parella, T., Inoue, T., Sprenger, G.A., Joglar, J., & Clapés, P. (2006) Fructose-6-phosphate aldolase in organic synthesis: preparation of D-fagomine, N-alkylated derivatives and preliminary biological assays. Organic Letters, 8: 6067-6070.

Samland, A.K., Wang, M., & Sprenger, G.A. (2008) MJ0400 from Methanocaldococcus jannaschii exhibits fructose 1,6-bisphosphate aldolase activity. FEMS Microbiology Letters, 281: 36-41.

Schneider, S., Sandalova, T., Schneider, G., Sprenger, G.A., & Samland, A.K. (2008) Replacement of a phenylalanine by a tyrosine in the active site confers fructose 6-phosphate aldolase activity to the transaldolase of Escherichia coli and human origin. Journal Biological Chemistry, 283: 30064-30072.

Samland A.K., Sprenger G.A. (2009) Transaldolase: from Biochemistry to human disease. International Journal of Biochemistry & Cell Biology, 41: 1482-1494.

Johnen, S., Sprenger, G.A. (2009) Characterization of recombinant thiamine diphosphate-dependent phosphonopyruvate decarboxylase from Streptomyces viridochromogenes Tü494. Journal of Molecular Catalysis B:Enzymatic, 61: 39-46.

Kurutsch, A., Richter, M., Brecht, V., Sprenger, G.A., & Müller, M. (2009) MenD as a versatile catalyst for asymmetric synthesis. Journal of Molecular Catalysis B:Enzymatic, 283: 56-66.

Schneider, S., Gutiérrez, M., Sandalova, T., Schneider, G., Clapés, P., Sprenger, G.A., Samland, A.K. (2010) Redesigning the active site of transaldolase TalB from Escherichia coli: new variants with improved affinity towards non-phosphorylated substrates. ChemBioChem, 11: 681-690.

Clapés P., Fessner W-D., Sprenger, G.A., Samland, A.K. (2010) Recent progress in stereoselective synthesis with aldolases. Current Opinion in Chemical Biology, 14: 154-167.

Castillo, J.A., Guérard-Hélaine, C., Gutiérrez, M., Garrabou, X., Sancelme, M. Schürmann, M., Inoue, T., Hélaine, v., Charmantray, F., Gefflaut, T., Hecquet, L., Joglar, J., Clapés, P., Sprenger, G.A, Lemaire, M. (2010) A mutant D-Fructose-6-Phosphate aldolase (Ala129Ser) as a powerful improved biocatalyst for direct syntheses of nitrocyclitols and carbohydrates from dihydroxyacetone. Advanced Synthesis and Catalysis, 352: 1039-1046.

Rale, M., Schneider, S., Sprenger, G.A., Samland, A.K., Fessner, W-D. (2011) Broadening deoxysugar glycodiversity: natural and engineered transaldolases unlock a complementary substrate space. Chemistry, a European Journal, 17: 2623-2632.

Samland, A.K., Rale, M., Sprenger, G.A., Fessner, W-D. (2011) The transaldolase family: novel synthetic opportunities from an ancient enzyme scaffold. ChemBioChem, 12: 1454-1474.

Samland, A.K., Baier, S., Schürmann, M., Inoue, T., Huf, S., Schneider, G., Sprenger, G.A., Sandalova, T. (2012) Conservation of structure and mechanism within the transaldolase enzyme family. FEBS Journal, 279: 766-778.

Widmann, M., Pleiss, J., Samland, A.K. (2012) Computational tools for rational protein engineering of aldolases. Computational and Structural Biotechnology Journal, 2 (3) e201209016.

Sanchez-Moreno, I., Nauton, L., Théry, V., Pinet, A., Petit, J-L., de Berardinis, V., Samland, A.K., Guérard-Hélaine, C., Lemaire, M. (2012) FSAB: a new fructose-6-phosphate aldolase from Escherichia coli. Cloning, over-expression and comparative kinetic characterization with FSAA. Journal of Molecular Catalysis B: Enzymatic, 84:9-14.

Müller, M., Beigi, M., Fries, A.; Waltzer, S.; Sprenger, G.; Eggeling, L. (2013) TCA Cycle Involved Enzymes SucA and Kgd, as well as MenD: Efficient Biocatalysts for Asymmetric C–C Bond Formation. Organic Letters, 15:452-455.

Müller M., Sprenger, G.A., Pohl, M. (2013) C-C bond formation using ThDP-dependent lyases. Current Opinion in Chemical Biology, 17:261-270.

Stellmacher, L., Sandalova, T., Leptihn, S., Schneider, G., Sprenger, G.A., Samland, A.K. (2015) Acid-based catalyst discriminates between a fructose 6-phosphate aldolase and a transaldolase. ChemCatChem 7: 3140-3151.

Stellmacher, L., Sandalova, T., Schneider, S., Schneider, G., Sprenger, G.A., Samland, A.K. (2016) Novel mode of inhibition by D-tagatose-6-phosphate through a Heyns rearrangement in the active site of transaldolase B variants. Acta Crystallographica Section D, 72: 467-476.

Schapfl, M., Baier, S., Fries, A., Ferlaino S., Waltzer, S., Müller, M., Sprenger, G.A. (2018) Extended substrate range of thiamine diphosphate-dependent MenD enzyme by coupling of two C-C-bonding reactions. Applied Microbiology and Biotechnology, 102:8359-8372.

Fries, A., Mazzaferro, L.S., Grüning, B., Bisel, P., Stibal, K., Sprenger, G.A., Günther, S., Müller, M. (2019) Alteration of the route to menaquinone (vitamin K2) in E. coli towards unnatural chorismate-derived metabolites. ChemBioChem, 20:1672-1677.

Sánchez-Moreno, I., Trachtmann, N., Ilhan, S., Hélaine, V., Lemaire, M., Guérard-Hélaine, C., Sprenger, G.A. (2019) 2-ketogluconate kinase from Cupriavidus necator H16: purification, characterization and exploration of its substrate specificity. Molecules, 24:2393.

Guitart Font, E., Sprenger, G.A. (2020) Opening a novel biosynthetic pathway to dihydroxyacetone and glycerol in Escherichia coli mutants through expression of a gene variant (fsaAA129S) for fructose 6-phosphate aldolase. International Journal of Molecular Sciences, 21:9625.


Contributions to books:

Sprenger, G.A., Schürmann, Me., Schürmann, Ma., Johnen, S., Sprenger, G., Sahm, H., Inoue, T., Schörken, U. (2007) C-C-bonding microbial enzymes: thiamine diphosphate-dependent enzymes and class I aldolases. pp. 298-311. In Asymmetric Synthesis with Chemical and Biological Methods (D Enders, K-E Jaeger, Hg.) Wiley-VCH, Weinheim.

Clapés, P., Sprenger, G.A., Joglar, J. (2008) Novel Strategies in aldolase-catalyzed synthesis of iminosugars. pp. 299-311. In “Modern Biocatalysis: Stereoselective and environmentally friendly reactions” (W.D. Fessner, T. Anthonsen, eds.) Wiley-VCH Verlag, Weinheim.

Castillo, J.A., Parella, T., Inoue T., Sprenger, G.A., Joglar, J., Clapés, P. (2009) Synthesis of D-fagomine by aldol addition of dihydroxyacetone to N-Cbz-3-aminopropanal catalyzed by D-fructose-6-phosphate aldolase. pp. 212-217. In “Practical Methods for Biocatalysis and Biotransformations” (J. Whittall, P. W.Sutton, eds.). John Wiley & Sons, Chichester, U.K.

Samland, A.K., Sprenger, G.A. (2015) Synthetic potential for dihydroxyacetone utilizing aldolases. pp.783-816. In. (P. Grunwald, Hg.). Industrial Biocatalysis. Pan Stanford Publishing Pte. Ltd., Singapore.

Sprenger G.A.  (2017) Glycerol as Carbon Source for Production of Added-Value Compounds. Chapter 4, p. 93-123. In (G. Gosset, Hg.) Engineering of microorganisms for the production of chemicals and fuels from renewable resources. Springer Nature Verlag ISBN: 978-3-319-51728-5

(If authors from different institutes contributed to the paper, the IMB's co-authors are highlighted in bold)

Franke, D., Sprenger, G.A., & Müller, M. (2003a) Easy access to trans-3, 4-dihydroxy-3,4-dihydrocyclohexa-1,5-diene carboxylic acid with engineered strains of Escherichia coli. ChemBioChem, 4: 775-777.

Franke, D., Lorbach, V., Esser, S., Dose, C., Sprenger, G.A., Halfar, M., Thömmes, J., Müller, R., Takors, R., & Müller, M. (2003b) (5S, 6S)-Dihydroxy-cyclohexa-1,3-dienecarboxylic acid: microbial access with engineered cells of Escherichia coli and applicability as starting material in natural product synthesis. Chemistry, a European Journal, 9: 4188-4196.

Rüffer, N., Heidersdorf, U., Kretzers, I., Sprenger, G.A., Raeven, L., & Takors, R. (2004) Fully integrated L-phenylalanine separation and concentration using reactive-extraction with liquid-liquid centrifuges in a fed-batch process with E. coli. Bioprocess and Biosystems Engineering 26: 239-248.

Oldiges, M., Kunze, M., Degenring, D., Sprenger, G.A., & Takors, R. (2004) Stimulation, monitoring and analysis of pathway dynamics by metabolic profiling in the aromatic amino acid pathway. Biotechnology Progress, 20:1623-1633.

Blaudeck, N., Kreutzenbeck, P., Müller, Ma., Sprenger, G.A. & Freudl, R. (2005) Isolation and characterization of bifunctional Escherichia coli TatA mutant proteins that allow efficient Tat-dependent protein translocation in the absence of TatB. Journal of Biological Chemistry, 280: 3426-3432.

Kreutzenbeck, P., Kröger, C., Lausberg, F. Blaudeck, N., Sprenger, G.A. & Freudl, R. (2007) Escherichia coli twin-arginine (Tat) mutant translocases possessing relaxed signal peptide recognition specificities. Journal of Biological Chemistry, 282: 7903-7911.

Sprenger GA (2007) From scratch to value: Engineering Escherichia coli wild type cells to the production of L-phenylalanine and other fine chemicals derived from chorismate. Applied Microbiology and Biotechnology, 75:739-749.

Albermann, C., Beuttler, H. (2008) Identification of the GDP-N-acetyl-D-perosamine producing enzymes from Escherichia coli O157 : H7. FEBS Letters, 582: 479-484.

Feuer, R., Ederer, M., Gilles, E.D., Sprenger, G.A., Sawodny, O., & Sauter, T. (2008) Analyse der evolutiven Adaptation am Beispiel einer pyruvat-auxotrophen Escherichia coli- Mutante. at- Automatisierungstechnik, 68: 56,257-268.

Albermann, C., Ghanegaonkar, S., Lemuth, K., Vallon, T., Reuss, M., Armbruster, W., & Sprenger, G.A. (2008) Biosynthesis of the vitamin E compound d-tocotrienol in recombinant Escherichia coli cells. ChemBioChem, 9: 2524-2533.

Vallon, T., Ghanegaonkar, S., Vielhauer, O., Müller, A. , Albermann, C., Sprenger, G., Reuss, M., Lemuth, K. (2008) Quantitative analysis of isoprenoid diphosphate intermediates in recombinant and wild-type Escherichia coli strains. Applied Microbiology and Biotechnology, 81: 175-182.

Albermann, C., Trachtmann, N., Sprenger, G.A. (2010) A simple and reliable method to conduct and monitor expression cassettes integration into the Escherichia coli chromosome. Biotechnology Journal, 5: 32-38.

Albermann, C. (2011) High versus low level expression of the lycopene biosynthesis genes from Pantoea ananatis in Escherichia coli. Biotechnology Letters, 33, 313-319.

Albermann, C. (2011) Integration von Expressionskassetten in das Chromosom von Escherichia coli. BIOspektrum, 17, 171-173.

Lemuth, K., Steuer, K., Albermann, C. (2011) Engineering of a plasmid-free Escherichia coli strain for improved in vivo biosynthesis of astaxanthin. Microbial Cell Factories, 10: 29.

Bongaerts, J., Esser, S., Lorbach, V., Al-Momani, L., Müller, M.A., Franke, D., Grondal, C., Kurutsch, A., Bujnicki, R., Takors, R., Raeven, L., Wubbolts, M., Bovenberg, R., Nieger, M., Schürmann, M., Trachtmann, N., Kozak, S., Sprenger, G.A., Müller, M. (2011) Biosynthesis as a model: diversity-oriented production of metabolites derived from chorismate and their use in organic synthesis. Angewandte Chemie, 123: 7927-7932.

Ghanegaonkar, S., Conrad, J., Beifuss, U., Sprenger, G.A., Albermann, C.(2012) Towards the in vivo production of tocotrienol compounds: engineering of a plasmid free Escherichia coli strain for the heterologous synthesis of 2-methyl-6-geranylgeranyl benzoquinol. Journal of Biotechnology, 164: 238-247.

Feuer, R., Gottlieb, K., Viertel, G., Klotz, J., Schober, S., Bossert, M., Sawodny, O., Sprenger, G., Ederer, M. (2012) Model-based analysis of an adaptive evolution experiment with Escherichia coli in a pyruvate limited continuous culture with glycerol. Eurasip Journal on Bioinformatics and Systems Biology, 2012:14.

Laschat, S., Roduner, E., Kaim, W., Sarkar, B., Urlacher, V.B., Pleiss, J. Gläser, G., Einicke, W.-D., Sprenger, G., Beifuß, U., Klemm,E.,Liebner, C., Hieronymus, H., Hsu, S.-F., Plietker, B. (2013) Selective Catalytic Oxidation of C–H Bonds with Molecular Oxygen. ChemCatChem, 5: 82-112.

Baumgärtner, F., Khan, L., Sprenger, G.A., Albermann, C. (2013) Construction of Escherichia coli strains with chromosomally integrated expression cassettes for the synthesis of 2-fucosyllactose. Microbial Cell Factories, 12:40.

Rodrigues, A.L., Trachtmann, N., Becker, J., Blotenberg, J., Lohanatha, A.F., Bolten, C.J., Corneli, C., de Souza Lima, A.O., Porto, L.M., Sprenger, G.A., Wittmann, C. (2013) Systems metabolic engineering of Escherichia coli for production of the antitumor drugs violacein and deoxyviolacein. Metabolic Engineering, 20: 29-41.

Weiner, M., Albermann, C., Gottlieb, K., Sprenger, G.A., Weuster-Botz, D. (2014a) Fed-batch production of L-phenylalanine from glycerol and ammonia with recombinant Escherichia coli. Biochemical Engineering Journal, 83: 62-69.

Weiner, M., Tröndle, J. , Albermann, C., Sprenger, G.A., Weuster-Botz, D. (2014b) Improvement of constraint-based flux estimation during L-phenylalanine production with Escherichia coli using targeted knock-out mutants. Biotechnology and Bioengineering, 111: 1406-1416.

Gottlieb K, Albermann C, Sprenger, G.A. (2014) Improvement of L-phenylalanine production from glycerol by recombinant Escherichia coli strains: the role of extra copies of glpK, glpX, and tktA genes. Microbial Cell Factories, 13: 96.

Baumgärtner, F., Conrad, J., Sprenger, G.A., Albermann, C. (2014) Synthesis of the human milk oligosaccharide lacto-N-tetraose in metabolically engineered, plasmid-free E. coli. ChemBioChem, 15: 1896-1900.

Weiner, M., Tröndle, J., Albermann, C., Sprenger, G.A., Weuster-Botz, D. (2014c) Carbon storage in recombinant Escherichia coli during growth on glycerol and lactic acid. Biotechnology and Bioengineering, im Druck.

Albermann, C., Weiner, M., Tröndle, J. , Weuster-Botz, D., Sprenger, G.A. (2014) Utilization of organophosphate:phosphate antitransporter for isotope labeling experiments in E. coli. FEMS Microbiology Letters, im Druck.

Weiner, M. Tröndle, J., Schmideder, A., Albermann, C., Binder, K., Sprenger, G.A., Weuster-Botz, D. (2015) Parallelized small-scale production of uniformly 13C-labeled cell-extract for quantitative metabolome analysis. Analytical Biochemistry, 478: 134-140.

Baumgärtner, F., Sprenger, G.A., Albermann, C. (2015a) Galactose-limited fed-batch cultivation of Escherichia coli for the production of lacto-N-tetraose. Enzyme Microbial Technology, 75-76: 37-43.

Baumgärtner, F., Jurzitza, L., Conrad, J., Beifuss, U., Sprenger, G.A., Albermann, C. (2015b) Synthesis of fucosylated lacto-N-tetraose using whole-cell biotransformation. Bioorganic & Medicinal Chemistry 23: 6799-6806.

Weiner M., Tröndle J., Albermann C., Sprenger G.A., Weuster-Botz, D. (2016) Perturbation experiments: Approaches for metabolic pathway analysis in bioreactors. Advances in Biochemical Engineering/Biotechnology, 152: 91–136.

Albermann, C., Beuttler H (2016) Synthesis of ß-carotene and other important carotenoids with bacteria. In (EJ. Vandamme, JL Revuelta, eds.) Industrial Biotechnology of Vitamins, Biopigments, and Antioxidants, chapter 9.   DOI 10.1002/9783527681754.ch9.

Trachtmann, N., Alvarez Fong, K.F., Guitart Font, E.Sprenger, G.A. (2016) Construction of chromosomally encoded lacZ and gfp reporter strains of Escherichia coli for the study of global regulation of metabolism. Engineering in Life Sciences 16: 675-681.

Weiner, M., Tröndle, J., Albermann, C.Sprenger, G.A., Weuster-Botz, D. (2017) Metabolic control analysis of L-phenylalanine production from glycerol with engineered E. coli using data from short-term steady-state perturbation experiments. Biochemical Engineering Journal, 126: 86-100.

Förster-Fromme, K., Schneider, S., Sprenger, G.A., Albermann, C. (2017) Functional expression of a human GDP-L-fucose transporter in the bacterium E. coli. Biotechnology Letters 39: 219-226.

Sprenger G.A., Baumgärtner F., Albermann, C. (2017) Production of human milk oligosaccharides by enzymatic and whole-cell microbial biotransformations. Journal of Biotechnology, 258: 79-91.

Sprenger G.A.  (2017) Glycerol as Carbon Source for Production of Added-Value Compounds. Chapter 4, p. 93-123. In (G. Gosset, Hg.) Engineering of microorganisms for the production of chemicals and fuels from renewable resources. Springer Nature Verlag ISBN: 978-3-319-51728-5.

Feuer, R., Gottlieb, K., Klotz, J., von Wulffen, J., Bossert, M., Sprenger, G., Sawodny, O. (2018) The Evolutive Adaptation of the Transcriptional Information Transmission in Escherichia coli. Chapter 6, p.161-179. In (M. Bossert, Hg.) Information- and Communication Theory in Molecular Biology (InKoMBio). Springer Verlag,  ISBN 978-3-319-54728-2.

Tröndle, J., Albermann, C., Weiner, M., Sprenger, G.A., Weuster-Botz, D. (2018) Phosphoenolpyruvate transporter enables targeted perturbation during metabolic analysis of L-phenylalanine production with Escherichia coli. Biotechnology Journal, im Druck. DOI 10.1002/biot.201700611.

Mohammadi Nargesi, B., Trachtmann, N., Sprenger, G.A., Youn, J-W. (2018) Production of p-amino-L-phenylalanine (L-PAPA) from glycerol by metabolic grafting of Escherichia coli. Microbial Cell Factories, 17:149.

Tröndle, J., Trachtmann, N.Sprenger, G.A., Weuster-Botz, D. (2018) Fed-batch production of L-tryptophan from glycerol using recombinant Escherichia coli. Biotechnology and Bioengineering,115:2881-2892.

Mohammadi Nargesi, B., Sprenger, G.A., Youn, J-W. (2019) Metabolic Engineering of Escherichia coli for para-amino-phenylethanol and para-amino-phenylacetic acid biosynthesis. Frontiers in Bioengineering and Biotechnology, 6:201.

Palanisamy, N., Degen, A., Morath, A., Ballestin, J.B., Juraske, C., Öztürk, M.A., Sprenger, G.A., Youn, J-Y.; Schamel, W.W., Di Ventura, B. (2019) SiMPl: Split intein-mediated selection of cells containing two plasmids using a single antibiotic. Nature Communications, 10:4967.

Tröndle, J., Schoppel, K., Bleidt, A., Trachtmann, N., Sprenger, G.A., Weuster-Botz, D. (2020) Metabolic control analysis of L-tryptophan production with Escherichia coli based on data from short-term perturbation experiments. Journal of Biotechnology, 307:15-28.

Youn, J-W., Albermann, C., Sprenger, G.A. (2020) In vivo cascade catalysis  of aromatic amino acids to mandelic acids using recombinant E. coli cells expressing hydroxymandelate synthase (HMS) from  Amycolatopsis mediterranei. Molecular Catalysis, 483:110713.

Moosmann, D., Mokeev, V., Kulik, A., Osipenkov, N., Kocadinc, S., Ort-Winklbauer, R., Handel, F., Hennrich, O., Youn, J-W., Sprenger, G.A., Mast, Y. (2020) Genetic engineering approaches for the fermentative production of phenylglycines. Applied Microbiology and Biotechnology, 104:3433–3444.

Guitart Font, E., Sprenger, G.A. (2020) Opening a novel biosynthetic pathway to dihydroxyacetone and glycerol in Escherichia coli mutants through expression of a gene variant (fsaAA129S) for fructose 6-phosphate aldolase. International Journal of Molecular Sciences, 21:9625. 

Schoppel, K., Trachtmann, N., Mittermeier, F., Sprenger, G.A., Weuster-Botz, D. (2021) Metabolic control analysis of L-tryptophan producing Escherichia coli applying targeted perturbation with shikimate. Bioprocess and Biosystems Engineering. 44:2591-2613.   



Contributions to books:

Lorbach, V., Franke, D., Esser, S., Dose, C., Sprenger, G.A., & Müller, M. (2004) Microbially produced functionalized cyclohexadiene-trans-diols as a new class of chiral building blocks in organic synthesis: On the way to green and combinatorial chemistry. p. 511-525. In Highlights in Bioorganic Chemistry: Methods and Applications (C. Schmuck & H. Wennemers, eds.) Wiley-VCH.

Sprenger, G.A., & Swings, J. (2005) Genus Zymomonas, In Garrity, G.M. (Hg.) Bergey´s Manual of Systematic Bacteriology, Second edition,Vol. 2, pp.282-286. The Proteobacteria, Springer Verlag, New York.

Sprenger, G.A. (2007) Aromatic Amino Acids. pp. 93-127. In Amino Acid Biosynthesis – Pathways, Regulation and Metabolic Engineering (Microbiology Monographs Vol.5/2007) (Wendisch, V., Hg.) Springer Verlag, Berlin Heidelberg.



This image shows Georg Sprenger

Georg Sprenger

Prof. Dr.

Former Head of the Institute for Microbiology (Retired)

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