GRK 1166:  Biokatalyse in unkonventionellen Medien - Ionische Flüssigkeiten, organische Lösungsmittel, überkritische Fluide und Gase als Reaktionsphasen für biokatalysierte Synthesen

• Fachliche Zuordnung: Verfahrenstechnik, Technische Chemie
• Förderung: Förderung von 2005 bis 2014
• Projektkennung: Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 811503

• Erstellungsjahr: 2015

Zusammenfassung der Projektergebnisse

Biocatalysis is gaining more and more importance in the sustainable provision of building blocks for pharmaceutical compounds and fine chemicals due to its well known advantages of excellent chemoselectivity, enantioselectivity, and mild (aqueous) reaction conditions. However, the use of aqueous systems limits the implementation of biocatalysis within the chemical industry. Water is rarely a good solvent specifically for hydrophobic substrates, limiting productivity and space time yield of the possible processes. Moreover, water may interfere with other reaction steps and/or downstream processing, thus hampering the direct substitution of chemical process steps with biocatalytic steps. Therefore, the Research Training Group biocatalysis using non-conventional media promoted the interdisciplinary education and research of young researchers in this highly topical research field spanning across biology, chemistry and biochemical engineering. The research programme addressed in particular the mechanisms of enzyme deactivation by nonconventional media, and their adaptation to these non-conventional conditions. Initially, this was mainly accomplished by evolution, later by rational approaches. Suitable test systems were developed that reproduced in small scale the special conditions in non-conventional media during technical use and allowed for a deeper understanding of biocatalyst medium interactions. In an integrated approach, case studies of biocatalytic reactions, which benefit from the use of nonconventional media were identified, optimised and described. The resulting information contributed to the rational understanding of the specific interactions between biocatalysts, media, and reactors which was used to develop design criteria for both biocatalysts and reaction systems. An interdisciplinary qualification programme promoted not only the research reults, but also the personal development and skills of the young researchers. The programme contained typical elements of a mandatory interdisciplinary lecture series, lectures selected complementary to the young researchers own qualification, seminars, biennial workshops, and soft-skill training. Specifically successful elements were on the one hand extension courses, 1-2 days topical lectures by (inter)- national guest researchers, where both content and organisation lay in the hands of the young researchers. On the other hand, tandem supervision by supervisors from different fields promoted the immersion into the respective complementary discipline. Besides the presentations at international conferences and publications, the RTG BioNoCo young researchers organised two summer schools and two lecture and poster sessions at Biotrans 2011 and 2013 to further promote BioNoCos visibility.

Projektbezogene Publikationen (Auswahl)

• 2006. Maximise equilibrium conversion in biphasic catalysed reactions: How to obtain reliable data for equilibrium constants? Adv. Synth. Catal. 348:1597–1604
  Eckstein MF, Lembrecht J, Schumacher J, Eberhard W, Spiess AC, Peters M, Roosen C, Greiner L, Leitner W, Kragl U
  
• 2006. Maximise equilibrium conversion in biphasic catalysed reactions: Mathematical description and practical guideline. Adv. Synth. Catal. 348:1591–1596
  Eckstein MF, Peters M, Lembrecht J, Spiess AC, Greiner L
  
• 2006. Select the best: novel biocatalysts for industrial applications. Trends Biotechnol. 24:248–250
  Konarzycka-Bessler M, Jaeger KE
  
• 2006. Selective aerobic oxidation in supercritical carbon dioxide catalyzed by the H5PV2Mo10O40 polyoxometalate. Chem. Commun.:2230–2232
  Maayan G, Ganchegui B, Leitner W, Neumann R
  
• 2007. Exploring conversion of biphasic catalytic reactions: Analytical solution and parameter study. Ind. Eng. Chem. Res. 46:7073–7078
  Peters M, Eckstein MF, Hartjen G, Spiess AC, Leitner W, Greiner L
  
• 2008. A computational approach to solvent selection for biphasic reaction systems; Dissertation, RWTH Aachen University
  Peters M
  
• 2008. Biocatalytic Carbon Nitrogen Double Bond Reduction; Dissertation, RWTH Aachen University
  Sibilla F
  
• 2008. Ilustrating computational solvent screening: Prediction of standard Gibbs energies of reaction in solution. AIChE J. 54:2729–2734
  Peters M, Greiner L, Leonhard K
  
• 2008. Lipase catalyzed synthesis of ester-based surfactants from biomass derivatives. Biofuels, Bioprod. Biorefining 2:144–154
  Karmee SK
  
• 2008. Prediction of partition coefficients using COSMO-RS: Solvent screening for maximum conversion in biocatalytic two-phase reaction systems. Chem. Eng. Process. 47:1034–1041
  Spieß AC, Eberhard W, Peters M, Eckstein MF, Greiner L, Büchs J
  
• 2008. Rational protein design of ThDP-dependent enzymes-engineering stereoselectivity. ChemBioChem 9:406–412
  Gocke D, Walter L, Gauchenova E, Kolter G, Knoll M, Berthold CL, Schneider G, Pleiss J, Müller M, Pohl M
  
• 2008. Systematic approach to solvent selection for biphasic systems with a combination of COSMO-RS and a dynamic modeling tool. Eng. Life Sci. 8:546–552
  Peters M, Zavrel M, Kahlen J, Schmidt T, Ansorge-Schumacher MB, Leitner W, Büchs J, Greiner L, Spiess AC
  
• 2008. Technical aspects of biocatalysis in non-CO2-based supercritical fluids. Biotechnol. J. 3:104–111
  Karmee SK, Casiraghi L, Greiner L
  
• 2008. Untersuchungen zum Inaktivierungsmechanismus von mikrobiellen Lipasen in wasserfreien Transesterifizierungen; Dissertation, Heinrich-Heine-Universität Düsseldorf
  Franken B
  
• 2009. Biocatalytic synthesis of ascorbyl esters and their biotechnological applications. Appl. Microbiol. Biotechnol. 81:1013–1022
  Karmee SK
  
• 2009. Biphasic mini-reactor for characterization of biocatalyst performance. Biotechnol. J. 4:44–50
  van den Wittenboer A, Schmidt T, Müller P, Ansorge-Schumacher MB, Greiner L
  
• 2009. Characterization of benzaldehyde lyase and benzoylformate decarboxylase in nonconventional media; Dissertation, Heinrich-Heine-Universität Düsseldorf
  Kokova M
  
• 2009. Chemo-enzymatic cascade oxidation in supercritical carbon dioxide/water biphasic media. Green Chem. 11:1052
  Karmee SK, Roosen C, Kohlmann C, Lütz S, Greiner L, Leitner W
  
• 2009. Comparative characterisation of thiamin diphosphate-dependent decarboxylases. J. Mol. Catal. B Enzym. 61:30–35
  Gocke D, Graf T, Brosi H, Frindi-Wosch I, Walter L, Müller M, Pohl M
  
• 2009. Encapsulation of synthetically valuable biocatalysts into polyelectrolyte multilayer systems. Langmuir 25:618–623
  Wiemann LO, Buthe A, Klein M, van den Wittenboer A, Dähne L, Ansorge-Schumacher MB
  
• 2009. Investigation of the carboligase activity of thiamine diphosphate-dependent enzymes using kinetic modeling and NMR spectroscopy. J. Mol. Catal. B Enzym. 61:73–79
  Kokova M, Zavrel M, Tittmann K, Spiess AC, Pohl M
  
• 2009. On the biocatalytic cleavage of silicon-oxygen bonds: A substrate structural approach to investigating the cleavage of protecting group silyl ethers by serine-triad hydrolases. J. Mol. Catal. B Enzym. 56:24–28
  Maraite A, Ansorge-Schumacher MB, Ganchegui B, Leitner W, Grogan G
  
• 2009. Stabilitäten der Benzaldehydlyase aus Pseudomonas fluorescens und der Carbonylreduktase aus Candida parapsilosis in wässrig-organischen Zweiphasensystemen; Dissertation, RWTH Aachen University
  van den Wittenboer A
  
• 2009. Substrate and water adsorption phenomena in a gas/solid enzymatic reactor. Biotechnol. J. 4:712–721
  Dimoula K, Pohl M, Büchs J, Spiess AC
  
• 2009. Thermodynamic and Kinetic Phenomena in the Enzymatic Conversion of Acetophenone to 1-(R)-Phenylethanol in a Continuous Gas/Solid Reactor; Dissertation, RWTH Aachen University
  Dimoula K
  
• 2009. Thiamin diphosphate in biological chemistry: exploitation of diverse thiamin diphosphate-dependent enzymes for asymmetric chemoenzymatic synthesis. FEBS J. 276:2894–2904
  Müller M, Gocke D, Pohl M
  
• 2010. Analysis of factors influencing enzyme activity and stability in the solid state Liliya Kulishova; Dissertation, Heinrich-Heine-Universität Düsseldorf
  Kulishova L
  
• 2010. Enzyme-catalyzed C–C bond formation using 2-methyltetrahydrofuran (2-MTHF) as (co)solvent: efficient and bio-based alternative to DMSO and MTBE. Green Chem. 12:2240
  Shanmuganathan S, Natalia D, van den Wittenboer A, Kohlmann C, Greiner L, Domínguez de María P
  
• 2010. Factors influencing the operational stability of NADPH-dependent alcohol dehydrogenase and an NADH-dependent variant thereof in gas/solid reactors. J. Mol. Catal. B Enzym. 67:271–283
  Kulishova L, Dimoula K, Jordan M, Wirtz A, Hofmann D, Santiago-Schübel B, Fitter J, Pohl M, Spiess AC
  
• 2010. Nanoparticle catalysed oxidation of sulfides to sulfones by in situ generated H2O2 in supercritical carbon dioxide/water biphasic medium. Chem. Commun. 46:6705–6707
  Karmee SK, Greiner L, Kraynov A, Müller TE, Niemeijer B, Leitner W
  
• 2010. Screening of new solvents for artemisinin extraction process using ab initio methodology. Green Chem. 12:241
  Lapkin AA, Peters M, Greiner L, Chemat S, Leonhard K, Liauw MA, Leitner W
  
• 2010. Systematic assessment of the stability of benzaldehyde lyase in aqueous–organic biphasic systems and its stabilization by modification with methoxy-poly(ethylene) glycol. J. Mol. Catal. B Enzym. 67:208–213
  van den Wittenboer A, Niemeijer B, Karmee SK, Ansorge-Schumacher MB
  
• 2011. Asymmetric reduction of ketones with recombinant E. coli whole cells in neat substrates. Chem. Commun. 47:12230–12232
  Jakoblinnert A, Mladenov R, Paul A, Sibilla F, Schwaneberg U, Ansorge-Schumacher MB, Dominguez de María P
  
• 2011. Cloning and characterization of a thermostable and halo-tolerant endoglucanase from Thermoanaerobacter tengcongensis MB4. Appl. Microbiol. Biotechnol. 89:315–326
  Liang C, Xue Y, Fioroni M, Rodríguez-Ropero F, Zhou C, Schwaneberg U, Ma Y
  
• 2011. Direct spectrophotometric assay for benzaldehyde lyase activity. Biotechnol. Res. Int.:478925
  Natalia D, Kohlmann C, Ansorge-Schumacher MB, Greiner L
  
• 2011. Directed evolution of a thermophilic endoglucanase (Cel5A) into highly active Cel5A variants with an expanded temperature profile. J. Biotechnol. 154:46–53
  Liang C, Fioroni M, Rodríguez-Ropero F, Xue Y, Schwaneberg U, Ma Y
  
• 2011. Einflussfaktoren auf die Stabilität und Aktivität der Benzaldehydlyase aus Pseudomonas fluorescens in Carboligasereaktionen mit aromatischen Aldehyden; Dissertation, Heinrich-Heine-Universität Düsseldorf
  Schwarz M
  
• 2011. Hydroxynitrile lyase from Arabidopsis thaliana: Identification of reaction parameters for enantiopure cyanohydrin synthesis by pure and immobilized catalyst. Adv. Synth. Catal. 353:2399–2408
  Okrob D, Paravidino M, Orru RVA, Wiechert W, Hanefeld U, Pohl M
  
• 2011. Ionic liquids in biotransformations: from proof-of-concept to emerging deep-eutectic-solvents. Curr. Opin. Chem. Biol. 15:220–225
  Domínguez de María P, Maugeri Z
  
• 2011. Mechanism of acetaldehyde-induced deactivation of microbial lipases. BMC Biochem. 12:10
  Franken B, Eggert T, Jaeger KE, Pohl M
  
• 2011. Nanocompartments with a pH release system based on an engineered OmpF channel protein. Soft Matter 7:532
  Ihle S, Onaca O, Rigler P, Hauer B, Rodríguez-Ropero F, Fioroni M, Schwaneberg U
  
• 2011. S-Selective mixed carboligation by structure-based design of the pyruvate decarboxylase from Acetobacter pasteurianus. ChemCatChem 3:1587–1596
  Rother neé Gocke D, Kolter G, Gerhards T, Berthold CL, Gauchenova E, Knoll M, Pleiss J, Müller M, Schneider G, Pohl M
  
• 2011. Utilizing high-throughput experimentation to enhance specific productivity of an E.coli T7 expression system by phosphate limitation. BMC Biotechnol. 11:22
  Huber R, Roth S, Rahmen N, Büchs J
  
• 2012. A rhodium complexlinked β-barrel protein as a hybrid biocatalyst for phenylacetylene polymerization. Chem. Commun. 48:9756–9758
  Onoda A, Fukumoto K, Arlt M, Bocola M, Schwaneberg U, Hayashi T
  (Siehe online unter https://doi.org/10.1039/c2cc35165j)
• 2012. A sugar isomerization reaction established on various (βα) 8-barrel scaffolds is based on substrate-assisted catalysis. Protein Eng. Des. Sel. 25:751–760
  Reisinger B, Bocola M, List F, Claren J, Rajendran C, Sterner R
  (Siehe online unter https://doi.org/10.1093/protein/gzs080)
• 2012. Benzaldehyde Lyase Catalysed Carboligation of 2-Furaldehyde into (R)-2,2’-Furoin in Non-Conventional Media; Dissertation, RWTH Aachen University
  Natalia D
  
• 2012. Einfluss unkonventioneller Medien auf die Selektivität ThDP-abhängiger Enzyme; Dissertation, Heinrich-Heine-Universität Düsseldorf
  Gerhards T
  
• 2012. Fluoreszenzreporterproteine als Werkzeuge in der Biotechnologie; Dissertation, Heinrich-Heine-Universität Düsseldorf
  Scholz KE
  
• 2012. Influence of organic solvents on enzymatic asymmetric carboligations. Adv. Synth. Catal. 354:2805–2820
  Gerhards T, Mackfeld U, Bocola M, von Lieres E, Wiechert W, Pohl M, Rother D
  
• 2012. Lipase catalyzed in situ production of acetaldehyde: A controllable and mild strategy for multi-step reactions. ChemCatChem 4:617–619
  Pérez-Sánchez M, Domínguez de María P
  (Siehe online unter https://doi.org/10.1002/cctc.201100493)
• 2012. Novel choline-chloride-based deep-eutectic-solvents with renewable hydrogen bond donors: levulinic acid and sugar-based polyols. RSC Adv. 2:421–425
  Maugeri Z, Domínguez de María P
  (Siehe online unter https://doi.org/10.1039/c1ra00630d)
• 2012. Organocatalytic synthesis of novel purine and pyrimidine acyclic nucleosides. Tetrahedron Lett. 53:6797–6800
  Palazzolo MA, Pérez-Sánchez M, Iribarren AM, Lewkowicz ES, Domínguez de María P
  (Siehe online unter https://doi.org/10.1016/j.tetlet.2012.10.009)
• 2012. Oxidationhydroxymethylation-reduction: a one-pot three-step biocatalytic synthesis of optically active α-aryl vicinal diols. Green Chem. 14:94
  Shanmuganathan S, Natalia D, Greiner L, Domínguez de María P
  (Siehe online unter https://doi.org/10.1039/c1gc16092c)
• 2012. Practical separation of alcohol-ester mixtures using deep-eutectic-solvents. Tetrahedron Lett. 53:6968–6971
  Maugeri Z, Leitner W, Domínguez de María P
  (Siehe online unter https://doi.org/10.1016/j.tetlet.2012.10.044)
• 2012. Reaction and Protein Engineering Employing a Carbonyl Reductase from Candida parapsilosis; Dissertation, RWTH Aachen University
  Jakoblinnert A
  
• 2012. Reengineering CelA2 cellulase for hydrolysis in aqueous solutions of deep eutectic solvents and concentrated seawater. Green Chem. 14:2719–2726
  Lehmann C, Sibilla F, Maugeri Z, Streit WR, Domínguez de María P, Martinez R, Schwaneberg U
  (Siehe online unter https://doi.org/10.1039/c2gc35790a)
• 2012. Stability, activity, and selectivity of benzaldehyde lyase in supercritical fluids. J. Supercrit. Fluids 62:173–177
  Natalia D, Greiner L, Leitner W, Ansorge-Schumacher MB
  (Siehe online unter https://doi.org/10.1016/j.supflu.2011.11.025)
• 2012. Structural and dynamical analysis of an engineered FhuA channel protein embedded into a lipid bilayer or a detergent belt. J. Struct. Biol. 177:291–301
  Rodríguez-Ropero F, Fioroni M
  
• 2012. Synthesis of chiral cyanohydrins by recombinant Escherichia coli cells in a micro-aqueous reaction system. Appl. Environ. Microbiol. 78:5025–5027
  Scholz KE, Okrob D, Kopka B, Grünberger A, Pohl M, Jaeger K-E, Krauss U
  (Siehe online unter https://doi.org/10.1128/AEM.00582-12)
• 2012. Tailoring a stabilized variant of hydroxynitrile lyase from Arabidopsis thaliana. ChemBioChem 13:797–802
  Okrob D, Metzner J, Wiechert W, Gruber K, Pohl M
  (Siehe online unter https://doi.org/10.1002/cbic.201100619)
• 2012. Who’s who? Allocation of carbonyl reductase isoenzymes from Candida parapsilosis by combining bio- and computational chemistry. ChemBioChem 13:803–809
  Jakoblinnert A, Bocola M, Bhattacharjee M, Steinsiek S, Bönitz-Dulat M, Schwaneberg U, Ansorge- Schumacher MB
  (Siehe online unter https://doi.org/10.1002/cbic.201200023)
• Optimierung der Hydroxynitril-Lyase aus Arabidopsis thaliana für die enantio-selektive Synthese von (R)-Cyanhydrinen – Entwicklung und Etablierung geeigneter Reaktionsparameter und molekulare Stabilisierung durch rationales Enzymdesign. Dissertation, Heinrich-Heine-Universität Düsseldorf
  Okrob D
  
• 2013. 2-Methyltetrahydrofuran and cyclopentylmethylether: Two green solvents for efficient purification of membrane proteins like FhuA. J. Chromatogr. B A 937:13–17
  Tenne SJ, Kinzel J, Arlt M, Sibilla F, Bocola M, Schwaneberg U
  (Siehe online unter https://doi.org/10.1016/j.jchromb.2013.07.021)
• 2013. A hybrid ring-opening metathesis polymerization catalyst based on an engineered variant of the β-barrel protein FhuA. Chem. - A Eur. J. 19:13865–13871
  Philippart F, Arlt M, Gotzen S, Tenne SJ, Bocola M, Chen HH, Zhu L, Schwaneberg U, Okuda J
  (Siehe online unter https://doi.org/10.1002/chem.201301515)
• 2013. Benzaldehyde lyase-catalyzed diastereoselective C-C bond formation by simultaneous carboligation and kinetic resolution. Org. Biomol. Chem. 11:2000–2004
  Müller CR, Pérez-Sánchez M, Domínguez de María P
  (Siehe online unter https://doi.org/10.1039/c2ob27344f)
• 2013. Biocatalysis in biomassderived solvents: The Quest for fully sustainable chemical processes. Curr. Org. Chem. 17:1188– 1199
  Perez-Sanchez M, Sandoval M, Hernaiz MJ, Dominguez de Maria P
  (Siehe online unter https://doi.org/10.2174/1385272811317110006)
• 2013. Chymotrypsin-catalyzed peptide synthesis in deep eutectic solvents. European J. Org. Chem.:4223–4228
  Maugeri Z, Leitner W, Domínguez de María P
  (Siehe online unter https://doi.org/10.1002/ejoc.201300448)
• 2013. Design of an activity and stability improved carbonyl reductase from Candida parapsilosis. J. Biotechnol. 165:52–62
  Jakoblinnert A, van den Wittenboer A, Shivange AV, Bocola M, Heffele L, Ansorge-Schumacher M, Schwaneberg U
  
• 2013. Directed laccase evolution for improved ionic liquid resistance. Green Chem. 15:1348–1355
  Liu H, Zhu L, Bocola M, Chen N, Spiess AC, Schwaneberg U
  (Siehe online unter https://doi.org/10.1039/c3gc36899h)
• 2013. Enhanced EGFP fluorescence emission in presence of PEG aqueous solutions and PIB1000-PEG6000-PIB1000 copolymer vesicles. Biomed Res. Int. 2013:ID 329087
  Muhammad N, Kryuchkova N, Dworeck T, Rodríguez-Ropero F, Fioroni M
  (Siehe online unter https://doi.org/10.1155/2013/329087)
• 2013. Fusion of a flavin-based fluorescent protein to hydroxynitrile lyase from Arabidopsis thaliana improves enzyme stability. Appl. Environ. Microbiol. 79:4727–4733
  Scholz KE, Kopka B, Wirtz A, Pohl M, Jaeger KE, Krauss U
  (Siehe online unter https://doi.org/10.1128/AEM.00795-13)
• 2013. Lipase-catalyzed (trans)esterification of 5-hydroxy- methylfurfural and separation from HMF esters using deep-eutectic solvents. ChemSusChem 6:630–634
  Krystof M, Pérez-Sánchez M, Domínguez de María P
  (Siehe online unter https://doi.org/10.1002/cssc.201200931)
• 2013. Lipase-mediated oxidative delignification in non-aqueous media: Formation of de-aromatized lignin-oil and cellulase-accessible polysaccharides. ChemSusChem 6:251–255
  Wiermans L, Pérez-Sánchez M, Domínguez De María P
  (Siehe online unter https://doi.org/10.1002/cssc.201200704)
• 2013. Lipase-mediated selective oxidation of furfural and 5-hydroxymethylfurfural. ChemSusChem 6:826–830
  Krystof M, Pérez-Sánchez M, Dominguez de María P
  (Siehe online unter https://doi.org/10.1002/cssc.201200954)
• 2013. Metabolic studies of γ-polyglutamic acid production in Bacillus licheniformis by small-scale continuous cultivations. Biochem. Eng. J. 73:29–37
  Wilming A, Begemann J, Kuhne S, Regestein L, Bongaerts J, Evers S, Maurer KH, Büchs J
  
• 2013. Multistep oxidase-lyase reactions: Synthesis of optically active 2-hydroxyketones by using biobased aliphatic alcohols. ChemCatChem 5:2512–2516
  
  
• 2013. Optimal scanning of all single-point mutants of a protein. J. Comput. Biol. 20:990–997
  Nov Y, Fulton A, Jaeger K-E
  (Siehe online unter https://doi.org/10.1089/cmb.2013.0026)
• 2013. P450 BM3 crystal structures reveal the role of the charged surface residue Lys/Arg184 in inversion of enantioselective styrene epoxidation. Chem. Commun. 49:4694–4696
  Shehzad A, Panneerselvam S, Linow M, Bocola M, Roccatano D, Mueller-Dieckmann J, Wilmanns M, Schwaneberg U
  (Siehe online unter https://doi.org/10.1039/c3cc39076d)
• 2013. Redirecting catalysis from proteolysis to perhydrolysis in subtilisin Carlsberg. J. Biotechnol. 167:279–286
  Despotovic D, Vojcic L, Blanusa M, Maurer KH, Zacharias M, Bocola M, Martinez R, Schwaneberg U
  (Siehe online unter https://doi.org/10.1016/j.jbiotec.2013.06.017)
• 2013. Reengineered carbonyl reductase for reducing methyl-substituted cyclohexanones. Protein Eng. Des. Sel. 26:291–298
  Jakoblinnert A, Wachtmeister J, Schukur L, Shivange AV, Bocola M, Ansorge-Schumacher MB, Schwaneberg U
  (Siehe online unter https://doi.org/10.1093/protein/gzt001)
• 2013. Reengineering of subtilisin Carlsberg for oxidative resistance. Biol. Chem. 394:79–87
  Schwaneberg U, Vojcic L, Despotovic D, Maurer KH, Zacharias M, Bocola M, Martinez R
  (Siehe online unter https://doi.org/10.1515/hsz-2012-0210)
• 2013. Synthesis of natural fragrance jasminaldehyde using silica-immobilized piperazine as organocatalyst. Catal. Sci. Technol. 3:2732–2736
  Pérez-Sánchez M, Domínguez de María P
  (Siehe online unter https://doi.org/10.1039/c3cy00313b)
• 2014. Assessing biocatalysis for the synthesis of optically active tetrahydropyrazolo [1,5-alpha] pyrimidines (THPPs) as novel therapeutic agents. J. Mol. Catal. B Enzym. 100:1–6
  Fernández-Álvaro E, Esquivias J, Pérez-Sánchez M, Domínguez de María P, Remui MJ
  (Siehe online unter https://doi.org/10.1016/j.molcatb.2013.11.012)
• 2014. Benzaldehyde lyase (BAL)-catalyzed enantioselective CC bond formation in deep-eutectic-solvents-buffer mixtures. J. Mol. Catal. B Enzym. 107:120–123
  Maugeri Z, Domínguez de María P
  (Siehe online unter https://doi.org/10.1016/j.molcatb.2014.06.003)
• 2014. Deep Eutectic Solvents: Properties and Biocatalytic Applications; Dissertation, RWTH Aachen University
  Maugeri Z
  
• 2014. Eine einfache Strategie zur Reinigung und Immobilisierung von Biokatalysatoren; Dissertation, Heinrich-Heine-Universität Düsseldorf
  Kopka B
  
• 2014. Facile biocatalytic synthesis of a macrocyclic lactone in sub- and supercritical solvents. Biocatal. Biotransformation 32:125–131
  Karmee SK, Niemeijer B, Casiraghi L, Mlambo B, Lapkin A, Greiner L
  (Siehe online unter https://doi.org/10.3109/10242422.2014.893579)
• 2014. From gene towards selective biomass valorization: Bacterial β-etherases with catalytic activity on lignin-like polymers. ChemSusChem 7:3164–3171
  Picart P, Müller C, Mottweiler J, Wiermans L, Bolm C, Domínguez de María P, Schallmey A
  (Siehe online unter https://doi.org/10.1002/cssc.201402465)
• 2014. Von gezielter Oligomerisierung zu katalytisch aktiven inclusion bodies. Dissertation. Heinrich-Heine-Universität Düsseldorf
  Diener M
  
• 2014. Whole-cell biocatalysis in deep-eutectic-solvents/aqueous mixtures. ChemCatChem 6:1535–1537
  Maugeri Z, Domínguez de María P
  (Siehe online unter https://doi.org/10.1002/cctc.201400077)
• 2014. Whole-cell teabag catalysis for the modularisation of synthetic enzyme cascades in micro-aqueous systems. ChemCatChem 6:1051–1058
  Wachtmeister J, Jakoblinnert A, Kulig J, Offermann H, Rother D
  (Siehe online unter https://doi.org/10.1002/cctc.201300880)
• 2015. Carbonyl reductase of Candida parapsilosis–Stability analysis and stabilization strategy. J. Mol. Catal. B Enzym. 112:45– 53
  Grosch J-H, Loderer C, Jestel T, Ansorge-Schumacher M, Spieß AC
  (Siehe online unter https://doi.org/10.1016/j.molcatb.2014.12.001)
• 2015. Exchange of single amino acids at different positions of a recombinant protein affects metabolic burden in Escherichia coli. Microb. Cell Fact. 14:10
  Rahmen N, Fulton A, Ihling N, Magni M, Jaeger K-E, Büchs J
  (Siehe online unter https://doi.org/10.1186/s12934-015-0191-y)
• 2015. Exploring the protein stability landscape: Bacillus subtilis lipase A as a model for detergent tolerance. ChemBioChem 16:930–936
  Fulton A, Frauenkron-Machedjou VJ, Skoczinski P, Wilhelm S, Zhu L, Schwaneberg U, Jaeger K-E
  (Siehe online unter https://doi.org/10.1002/cbic.201402664)
• 2015. Investigation of structural determinants for the substrate specificity in the zinc-dependent alcohol dehydrogenase CPCR2 from Candida parapsilosis. ChemBioChe
  Loderer C, Dhoke G V, Davari MD, Kroutil W, Schwaneberg U, Bocola M, Ansorge-Schumacher MB
  (Siehe online unter https://doi.org/10.1002/cbic.201500100)
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