Prof. Dr. Rebecca Buller

Prof. Dr. Rebecca Buller

Prof. Dr. Rebecca Buller

ZHAW Life Sciences und Facility Management
Institut für Chemie und Biotechnologie
Einsiedlerstrasse 31
8820 Wädenswil

+41 (0) 58 934 54 38
rebecca.buller@zhaw.ch

Projekte

Publikationen

Beiträge in wissenschaftlicher Zeitschrift, peer-reviewed

  • Honda Malca, S. et al. (2026) ‘Discovery and engineering of polymerases and ligases for the synthesis of modified nucleic acids’, Current Opinion in Chemical Biology, 93(102697). doi: 10.1016/j.cbpa.2026.102697.
  • Özgen, F. F. et al. (2026) ‘Biomass-derived diformylxylose as a renewable solvent for biocatalysis applications’, ChemSusChem, 19(4), p. e202502273. doi: 10.1002/cssc.202502273.
  • Schaub, D. et al. (2026) ‘Toward the chemoenzymatic synthesis of DNA-encoded libraries’, ACS Central Science, 12(1), pp. 28–39. doi: 10.1021/acscentsci.5c01516.
  • Hecht, K. and Buller, R. (2025) ‘Industrializing biocatalysis’, Chimia, 79(7-8), pp. 522–527. doi: 10.2533/chimia.2025.522.
  • Graber, D. et al. (2025) ‘Resolving data bias improves generalization in binding affinity prediction’, Nature Machine Intelligence, 7(10), pp. 1713–1725. doi: 10.1038/s42256-025-01124-5.
  • Kumar, A. et al. (2025) ‘Streamlining enzyme discovery and development through data analysis and computation’, Chem Catalysis, 5(10), p. 101445. doi: 10.1016/j.checat.2025.101445.
  • Vornholt, T. et al. (2025) ‘Of revolutions and roadblocks : the emerging role of machine learning in biocatalysis’, ACS Central Science, 11(10), pp. 1828–1838. doi: 10.1021/acscentsci.5c00949.
  • Stockinger, P. et al. (2025) ‘Computational analysis reveals temperature-induced stabilization of FAST-PETase’, Computational and Structural Biotechnology Journal, 27, pp. 969–977. doi: 10.1016/j.csbj.2025.03.006.
  • Buller, R. et al. (2024) ‘Structure prediction and computational protein design for efficient biocatalysts and bioactive proteins’, Angewandte Chemie: International Edition, 64(2), p. e202421686. doi: 10.1002/anie.202421686.
  • Stockinger, P. and Buller, R. (2024) ‘Nature’s toolbox for the hydrolysis of lactams and cyclic imides’, ACS Catalysis, 14(21), pp. 16055–16073. doi: 10.1021/acscatal.4c04474.
  • Patsch, D. et al. (2024) ‘Enriching productive mutational paths accelerates enzyme evolution’, Nature Chemical Biology, 20(12), pp. 1662–1669. doi: 10.1038/s41589-024-01712-3.
  • Bopp, C. E. et al. (2024) ‘Elucidating the role of O2 uncoupling for the adaptation of bacterial biodegradation reactions catalyzed by Rieske oxygenases’, ACS Environmental Au, 4(4), pp. 204–218. doi: 10.1021/acsenvironau.4c00016.
  • André, A. et al. (2024) ‘A new physical and biological strategy to reduce the content of zearalenone in infected wheat kernels : the effect of cold needle perforation, microorganisms, and purified enzyme’, Food Research International, 186(114364). doi: 10.1016/j.foodres.2024.114364.
  • Honda Malca, S. et al. (2024) ‘Excelzyme : a Swiss university-industry collaboration for accelerated biocatalyst development’, Chimia, 78(3), pp. 108–117. doi: 10.2533/chimia.2024.108.
  • Honda Malca, S. et al. (2024) ‘Effective engineering of a ketoreductase for the biocatalytic synthesis of an ipatasertib precursor’, Communications Chemistry, 7(1), p. 46. doi: 10.1038/s42004-024-01130-5.
  • Eichenberger, M. et al. (2023) ‘The catalytic role of glutathione transferases in heterologous anthocyanin biosynthesis’, Nature Catalysis, 6(10), pp. 927–938. doi: 10.1038/s41929-023-01018-y.
  • Patsch, D. et al. (2023) ‘LibGENiE : a bioinformatic pipeline for the design of information-enriched enzyme libraries’, Computational and Structural Biotechnology Journal, 21, pp. 4488–4496. doi: 10.1016/j.csbj.2023.09.013.
  • Buller, R. et al. (2023) ‘From nature to industry : harnessing enzymes for biocatalysis’, Science, 382(6673), p. eadh8615. doi: 10.1126/science.adh8615.
  • Hegarty, E., Büchler, J. and Buller, R. M. (2023) ‘Halogenases for the synthesis of small molecules’, Current Opinion in Green and Sustainable Chemistry, 41(100784). doi: 10.1016/j.cogsc.2023.100784.
  • Giger, S. and Buller, R. (2023) ‘Advances in noncanonical amino acid incorporation for enzyme engineering applications’, Chimia, 77(6), pp. 395–402. doi: 10.2533/chimia.2023.395.
  • Patsch, D. and Buller, R. (2023) ‘Improving enzyme fitness with machine learning’, Chimia, 77(3), pp. 116–121. doi: 10.2533/chimia.2023.116.
  • Büchler, J. et al. (2022) ‘A collaborative journey towards the late‐stage functionalization of added‐value chemicals using engineered halogenases’, Helvetica Chimica Acta, 106(1), p. e202200128. doi: 10.1002/hlca.202200128.
  • Papadopoulou, A. et al. (2022) ‘Development of an ene reductase-based biocatalytic process for the production of flavor compounds’, Organic Process Research & Development, 26(7), pp. 2102–2110. doi: 10.1021/acs.oprd.2c00096.
  • Voss, M. et al. (2022) ‘Enzyme engineering enables inversion of substrate stereopreference of the halogenase WelO5*’, ChemCatChem, 14(24), p. e202201115. doi: 10.1002/cctc.202201115.
  • Papadopoulou, A., Meyer, F. and Buller, R. M. (2022) ‘Engineering Fe(II)/α-ketoglutarate-dependent halogenases and desaturases’, Biochemistry, 62(2), pp. 229–240. doi: 10.1021/acs.biochem.2c00115.
  • Büchler, J. et al. (2022) ‘Algorithm-aided engineering of aliphatic halogenase WelO5* for the asymmetric late-stage functionalization of soraphens’, Nature Communications, 13(371). doi: 10.1038/s41467-022-27999-1.
  • Eichenberger, M. et al. (2021) ‘Asymmetric cation-olefin monocyclization by engineered squalene-hopene cyclases’, Angewandte Chemie: International Edition, 60(50), pp. 26080–26086. doi: 10.1002/anie.202108037.
  • Reiter, M. et al. (2021) ‘Swiss women in chemistry – two years later ...’, Chimia, 75(12), pp. 1088–1090. doi: 10.2533/chimia.2021.1088.
  • Papadopoulou, A. et al. (2021) ‘Re‐programming and optimization of a L‐proline cis‐4‐hydroxylase for the cis‐3‐halogenation of its native substrate’, ChemCatChem, 13(18), pp. 3914–3919. doi: 10.1002/cctc.202100591.
  • Meyer, F. et al. (2021) ‘Modulating chemoselectivity in a Fe(II)/α-ketoglutarate-dependent dioxygenase for the oxidative modification of a non-proteinogenic amino acid’, ACS Catalysis, 2021(11). doi: 10.1021/acscatal.1c00678.
  • Hecht, K. et al. (2020) ‘Biocatalysis in the Swiss manufacturing environment’, Catalysts, 10(12), p. 1420. doi: 10.3390/catal10121420.
  • Voss, M. et al. (2020) ‘Multi‐faceted set‐up of a diverse ketoreductase library enables the synthesis of pharmaceutically‐relevant secondary alcohols’, ChemCatChem, 13(6), pp. 1538–1545. doi: 10.1002/cctc.202001871.
  • Aregger, D., Peters, C. and Buller, R. (2020) ‘Characterization of the novel ene reductase Ppo-Er1 from paenibacillus polymyxa’, Catalysts, 10(2). doi: 10.3390/catal10020254.
  • Voss, M., Honda Malca, S. and Buller, R. (2020) ‘Exploring the biocatalytic potential of Fe/α‐ketoglutarate dependent halogenases’, Chemistry - A European Journal. doi: 10.1002/chem.201905752.
  • Peters, C. and Buller, R. (2019) ‘Industrial application of 2-oxoglutarate-dependent oxygenases’, Catalysts, 9(3), pp. 221–240. doi: 10.3390/catal9030221.
  • Peters, C. and Buller, R. (2019) ‘Linear enzyme cascade for the production of (–)-iso-isopulegol’, Zeitschrift für Naturforschung C, 74(3-4). doi: 10.1515/znc-2018-0146.
  • Frey, R., Hayashi, T. and Buller, R. (2019) ‘Directed evolution of carbon–hydrogen bond activating enzymes’, Current Opinion in Biotechnology, 60, pp. 29–38. doi: 10.1016/j.copbio.2018.12.004.
  • Büchler, J., Papadopoulou, A. and Buller, R. (2019) ‘Recent advances in Flavin-dependent halogenase biocatalysis : sourcing, engineering, and application’, Catalysts, 9(12), p. 1030. doi: 10.3390/catal9121030.
  • Hayashi, T. et al. (2019) ‘Evolved aliphatic halogenases enable regiocomplementary C‐H functionalization of an added‐value chemical’, Angewandte Chemie: International Edition, 58(51), pp. 18535–18539. doi: 10.1002/anie.201907245.
  • Hayashi, T. et al. (2019) ‘Evolvierte aliphatische Halogenasen ermöglichen die regiokomplementäre C‐H‐Funktionalisierung einer hochwertigen Chemikalie’, Angewandte Chemie, 131(51), pp. 18706–18711. doi: 10.1002/ange.201907245.
  • Papadopoulou, A., Hecht, K. and Buller, R. (2019) ‘Enzymatic PET degradation’, Chimia, 73(9), pp. 743–749. doi: 10.2533/chimia.2019.743.
  • Peters, C. et al. (2019) ‘Novel Old Yellow Enzyme subclasses’, ChemBioChem. doi: 10.1002/cbic.201800770.
  • Kries, H., Blomberg, R. and Hilvert, D. (2013) ‘De novo enzymes by computational design’, Current Opinion in Chemical Biology, 17(2), pp. 221–228. doi: 10.1016/j.cbpa.2013.02.012.
  • Blomberg, R. et al. (2013) ‘Precision is essential for efficient catalysis in an evolved Kemp eliminase’, Nature, 503(7476), pp. 418–421. doi: 10.1038/nature12623.
  • Richter, F. et al. (2012) ‘Computational design of catalytic dyads and oxyanion holes for ester hydrolysis’, Journal of the American Chemical Society, 134(39), pp. 16197–16206. doi: 10.1021/ja3037367.
  • Privett, H. K. et al. (2012) ‘Iterative approach to computational enzyme design’, Proceedings of the National Academy of Sciences of the United States of America, 109(10), pp. 3790–3795. doi: 10.1073/pnas.1118082108.
  • Chapleau, R. R. et al. (2008) ‘Design of a highly specific and noninvasive biosensor suitable for real-time in vivo imaging of mercury (II) uptake’, Protein Science, 17(4), pp. 614–622. doi: 10.1110/ps.073358908.

Buchbeiträge, peer-reviewed

  • Hecht, K. and Buller, R. (2019) ‘Ene-reductases in pharmaceutical chemistry’, in Grunwald, P. (ed.) Pharmaceutical biocatalysis : chemoenzymatic synthesis of active pharmaceutical ingredients. Singapore: Jenny Stanford.
  • Buller, R. et al. (2017) ‘An appreciation of biocatalysis in the Swiss manufacturing environment’, in Biocatalysis : an industrial perspective. Royal Society of Chemistry, pp. 1–43. doi: 10.1039/9781782629993-00001.

Weitere Publikationen

  • Graber, D. et al. (2024) GEMS : a generalizable GNN framework for protein-ligand binding affinity prediction through robust data filtering and language model integration. bioRxiv. doi: 10.1101/2024.12.09.627482.
  • André, A. et al. (2024) ‘A new physical and biological strategy to reduce the content of zearalenone in infected wheat kernels : the effect of cold needle perforation, microorganisms, and purified enzyme’, in 11th Symposium on Recent Advances in Food Analysis (RAFA), Prague, Czech Republic, 5-8 November 2024.
  • Buller, R. et al. (2021) Chemistry roadmap for research infrastructures 2025-2028 by the Swiss chemistry community. Swiss Academy of Sciences. doi: 10.5281/zenodo.4572642.
  • Buller, R. (2021) ‘Biocatalysis and biosynthesis’, in Technology Outlook 2021. Swiss Academy of Engineering Sciences SATW, p. 71. Available at: https://www.satw.ch/de/publikationen/technology-outlook-2021.

Mündliche Konferenzbeiträge und Abstracts

  • André, A. et al. (2023) ‘Eine biologische Strategie zur Reduzierung des Zearalenongehalts in infizierten Weizenkörnern’, in 9. D-A-CH-Tagung für angewandte Getreidewissenschaften, Detmold, Deutschland, 5.-6. Oktober 2023.
  • André, A. et al. (2022) ‘Mycotoxins reduction strategies to reintroduce grain side product streams into the food value chain’, in 20th ICC Conference, Vienna, Austria, 5-7 July 2022.

Forschungsdaten

Özgen, Fatma Feyza; Stockinger, Peter; Komarova, Anastasia; Luterbacher, Jeremy; Buller, Rebecca, 2025. Dataset for biomass-derived diformylxylose as a renewable solvent for biocatalysis applications. Zenodo. Verfügbar unter: https://doi.org/10.5281/zenodo.17286566

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