Cui, H., Cai, H., Jaeger, K.-E., Davari, M.D., Schwaneberg, U. (2020) Computer-Assisted Recombination (CompassR) Teaches us how to recombine Beneficial Substitutions from Directed Evolution Campaigns. Chemistry doi: 10.1002/chem.201903394.

Perez-Garcia, P., Kobus, S., Hoeppner, A., Holzscheck, Strunk, C.H., Huber, H.N.H., Jaeger, K.-E., Kovacic, F., Smits, S., Streit, W.R., Chow, J. (2020) The origin of metallo-beta-lactamases: The highly promiscuous hydrolase Igni 18 from the crenarchaeon Ignicoccus hospitalis represents the paradigm of an ancestral enzyme. Acta Crystallogr F Struct Biol Commun Actions 75: 307-311  doi: 10.1107/S2053230X19002851

Viegas, A., Dollinger, P., Verma, N., Kubiak, J., Viennet, T., Seidel, C.A.M., Gohlke, H., Etzkorn, M., Kovacic, F., Jaeger, K.-E. (2020) Solution NMR structure of lipase binding domain MD1 of Pseudomonas aeruginosa foldase and its potential role in lipase folding. (“Structural and dynamic insights revealing how lipase binding domain MD1 of Pseudomonas aeruginosa foldase affects lipase activation”)Sci Rep.10: 1 doi: 10.1038/s41598-020-60093-4

Nutschel, C., Fulton, A., Zimmermann, O., Schwaneberg, U., Jaeger, K.-E., Gohlke, H. (2020) Systematically scrutinizing the impact of substitution sites on thermosability and detergent tolerance for Bacillus lipase A. J. Chem. Inform. and modeling NA, acs.jcim. 9b00954 doi: 10.1021/acs.jcim.9b00954

Ferrer, M., Méndez-Garcia, C., Bargiela, R., Chow, J., Alonso, S., Garcia-Moyano, A., Bjerga, G.E.K., Steen, I.H., Schwabe, T., Blom, C., Vester, J., Weckbecker, A., Shahgaldian, P., Carvalho de, C.CCR, Meskys, R., Zanaroli, G., Glöckner, F. O., Fernández-Guerra, A., Thambisetty, S., Calle de la, F., Golyshina, O.V., Yakimov, M.M., Jaeger, K.-E., Yakunin, A. F. Streit, W. R., McMeel, O., Calewaert, J-B., Tonné, N., Golyshin, P. N., INMARE Consortium (2019) Decoding the Ocean’s Microbiological Secrets for Marine Enzyme Biodiscovery. FEMS Microbiol. Lett. 366: 1  doi: 10.1093/femsle/fny285

Bollinger, A., Molitor, R., Thies, S., Koch, R., Coscolín, C., Ferrer, M., Jaeger, K.-E. (2020) Organic-Solvent Tolerant Carboxylic Ester Hydrolases for Organic Synthesis. Appl Environ Microbiol. 17: 86 Epub 0106-20 doi: 10.1128/AEM.00106-20

Bollinger, A., Thies, S., Katzke, N., Jaeger, K.-E. (2020) The biotechnological potential of marine bacteria in the novel lineage of Pseudomonas pertucinogena. Microb.Biotechnol doi: 10.1111/1751-7915.13288

Bollinger, A., Thies, S., Knieps-Grünhagen, E., Gertzen, C., Kobus, S., Höppner, A., Ferrer, M., Gohlke, H., Smits, Sander H J, Jaeger, K.-E. (2020) A Novel Polyester Hydrolase from the Marine Bacterium Pseudomonas Aestusnigri – Structural and Functional Insights. Front Microbiol. 11: 114 doi: 10.3389/fmicb.2020.00114.eCollection 2020

Kubicki, S., Bator, I., Jankowski, S., Schipper, K., Tiso, T., Feldbrügge, M., Blank, L. M., Thies, S., Jaeger, K.-E. (2020) A straightforward assay for screening and quantification of biosurfactats in microbial culture supernatants.Front. Bioeng. Biotechnol 8: 958 doi: 10.3389/fbioe.2020.00958

Tiso, T., Ihling, N., Kubicki, S., Biselli, A., Schonhoff, A. , Bator, I., Thies, S., Karmainski ,T., Kruth, S., Willenbrink, A.-L., Loeschcke, A., Zapp, P., Jupke, A., Jaeger, K.-E., Büchs, J., Blank, L.M. (2020) Integration of genetic and process engineering for optimized rhamnolipid production using Pseudomonas putida. Front. Bioeng. Biotechnol. 8: 976 doi:10.3389/fbioe.2020.00976

Chernomor, O., Peters, L., Schneidewind, J., Loeschcke, A., Knieps-Grünhagen, E., Schmitz, F., von Lieres, E., Kutta, R. J., Svensson, V., Jaeger, K.-E., Drepper, T., von Haeseler, A., Krauss, U.  (2020) Complex evolution of light-dependent protochlorophyllide oxidoreductases in aerobic anoxygenic phototrophs: origin, phylogeny and function. Mol Biol Evol. msaa234 doi:10.1093/molbev/msaa234

Lee, J., Hilgers, F., Loeschcke, A., Jaeger, K.-E., Feldbrügge, M. (2020) Ustilago maydis serves as a novel production host for the synthesis of plant and fungal sesquiterpenoids. Front. Microbiol. 11: 1655 doi:10.3389/fmicb.2020.01655

Hage-Hülsmann, J., Metzger, S., Wewer, V., Buechel, F., Troost, K., Thies, S., Loeschcke, A., Jaeger, K.-E., Drepper, T.  (2020) Biosynthesis of cycloartenol by expression of plant and bacterial oxidosqualene cyclases in engineered. Rhodobacter capsulatus J Biotechnol X 4: 100014 doi:10.1016/j.btecx.2020.100014

Weihmann, R., Domröse, A., Drepper, T., Jaeger, K.-E., Loeschcke, A. (2020) Protocols for yTREX/Tn5-based gene cluster expression in Pseudomonas putida. Microb Biotechnol. 1:250-262.doi: 10.1111/1751.13402. Epub2019 Jun 4.

Raber, H.F., Heerde, T., El Dinm S.N., Flaig, C., Hilgers, F., Bitzenhofer, N., Jaeger, K.-E., Drepper, T., Gottschalk, K.E., Bodenberger, N.E., Weil,T., Kubiczek, D.H., Rosenau, F. (2020) Azulitox-A Pseudomonas aeruginosa P28-Derived Cancer-Cell-Specific Protein Photosensitizer. Biomacromolecules; 21:5067-5076, doi: 10.1021/acs.biomac.0c01216

Hogenkamp, F., Hilgers, F., Knapp, A., Klaus, O., Bier, C., Binder, D., Jaeger, K.-E., Drepper, T., Pietruszka, J.  (2020) Effect of Photocaged Isopropyl β-d-1-thiogalactopyranoside Solubility on the Light Responsiveness of LacI-controlled Expression Systems in Different Bacteria. Chembiochem.  doi: 10.1002/cbic.202000377

Perez-Garcia, P., Kobus, S., Hoeppner, A., Holzscheck, N.,, Strunk, C.H., Huber, H.N.H., Jaeger, K.-E., Kovacic, F., Smits, S., Streit, W.R., Chow, J. (2020) The origin of metallo-beta-lactamases: The highly promiscuous hydrolase Igni 18 from the grenarchaeon Ignicoccus hospitalis represents the paradigm of an ancestral enzyme. Acta Crystallogr F Struct Biol Commun Actions 75: 307-311  doi: 10.1107/S2053230X19002851

Volkenborn, K., Kuschmierz, L., Benz, N., Lenz, P., Knapp, A., Jaeger, K.-E. (2020) The length of ribosomal binding site spacer sequence controls the production yield for intracellular and secreted proteins by Bacillus subtilis. Microbial cell factories, 19:1-12. doi: 10.1186/s12934-020-01404-2

Lamm, R., Jäger, V.D., Hyman, B., Berg, C., Cürten, C., Krauss, U., Jaeger, K.-E., Büchs, J. (2020) Detailed small-scale characterization and scale-up of active YFP inclusion body production with Escherichia coli induced by a tetrameric coiled coil domain. J Biosci Bioeng. 129:730-740. doi: 10.1016/j.jbiosc.2020.02.003. Epub 2020 Mar 3. PMID: 32143998

Jäger, V.D., Lamm, R., Küsters, K., Ölcücü, G., Oldiges, M., Jaeger, K.-E., Büchs, J., Krauss, U. (2020) Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application. Appl.MicrobBiotech. 104:7313-7329 doi: 10.1007/s00253-020-10760-3

Habash, S. S., Könen, P. P. Loeschcke, A., Wüst, M., Jaeger, K.-E., Drepper, T., Grundler, F.M.W., Schleker, A.S.S. (2020) The Plant Sesquiterpene Nootkatone Efficiently Reduces Heterodera schachtii Parasitism by Activating Plant Defense. Int J Mol Sci 21:9627. doi: 10.3390/ijms21249627