Scientific papers

  1. Wickerhamomyces subpelliculosus as whole-cell biocatalyst for stereoselective bioreduction of ketones

    Bódai V., Nagy-Győr L., Örkényi R., Molnár Z., Kohári S., Erdélyi B., Nagymáté Z., Romsics C., Paizs C., Poppe L., Hornyánszky G.
    Journal of Molecular Catalysis B: Enzymatic (2016) 134: 206-214
    DOI: 10.1016/j.molcatb.2016.11.003

  2. Aminated single-walled carbon nanotubes as carrier for covalent immobilization of phenylalanine ammonia-lyase

    Bartha-Vári J.H., Bencze L.C., Bell E., Poppe L., Katona G., Irimie F.-D., Paizs C., Toşa M.I.
    Periodica Polytechnica Chemical Engineering (2017) 61(1): 59-66
    DOI: 10.3311/PPch.10417

  3. A Methylidene Group in the Phosphonic Acid Analogue of Phenylalanine Reverses the Enantiopreference of Binding to Phenylalanine Ammonia-Lyases

    Bata Z., Qian R., Roller A., Horak J., Bencze L.C., Paizs C., Hammerschmidt F., Vértessy B.G., Poppe L.
    Advanced Synthesis and Catalysis (2017) 359(12): 2109-2120
    DOI: 10.1002/adsc.201700428

  4. A novel phenylalanine ammonia-lyase from Kangiella koreensis

    Varga A., Bata Z., Csuka P., Bordea D.M., Vértessy B.G., Marcovici A., Irimie F.D., Poppe L., Bencze L.C.
    Studia Universitatis Babes-Bolyai Chemia (2017) 62(3): 293-308
    DOI: 10.24193/subbchem.2017.3.25

  5. Optimization of 2-alkoxyacetates as acylating agent for enzymatic kinetic resolution of chiral amines

    Oláh M., Kovács D., Katona G., Hornyánszky G., Poppe L.
    Tetrahedron (2018) 74(27): 3663-3670
    DOI: 10.1016/j.tet.2018.05.032

  6. Tailored Mutants of Phenylalanine Ammonia-Lyase from Petroselinum crispum for the Synthesis of Bulky L- and D-Arylalanines

    Filip A., Nagy E.Z.A., Tork S.D., Bánóczi G., Toşa M.I., Irimie F.D., Poppe L., Paizs C., Bencze L.C.
    ChemCatChem (2018) 10(12): 2627-2633
    DOI: 10.1002/cctc.201800258

  7. Pseudomonas fluorescens Strain R124 Encodes Three Different MIO Enzymes

    Csuka P., Juhász V., Kohári S., Filip A., Varga A., Sátorhelyi P., Bencze L.C., Barton H., Paizs C., Poppe L.
    ChemBioChem (2018) 19(4): 411-418
    DOI: 10.1002/cbic.201700530

  8. Click reaction-aided enzymatic kinetic resolution of secondary alcohols

    Moisǎ M.E., Poppe L., Gal C.A., Bencze L.C., Irimie F.D., Paizs C., Peter F., Toşa M.I.
    Reaction Chemistry and Engineering (2018) 3(5): 790-798
    DOI: 10.1039/c8re00091c

  9. Continuous-flow enzymatic kinetic resolution mediated by a lipase nanobioconjugate

    Moisă M.E., Bencze L.C., Paizs C., Toşa M.I.
    Studia Universitatis Babes-Bolyai Chemia (2019) 64(2Tom1): 79-86
    DOI: 10.24193/subbchem.2019.2.07

  10. Mapping the Hydrophobic Substrate Binding Site of Phenylalanine Ammonia-Lyase from Petroselinum crispum

    Nagy E.Z.A., Tork S.D., Lang P.A., Filip A., Irimie F.D., Poppe L., Toşa M.I., Schofield C.J., Brem J., Paizs C., Bencze L.C.
    ACS Catalysis (2019) 9(9): 8825-8834
    DOI: 10.1021/acscatal.9b02108

  11. Conservation of the biocatalytic activity of whole yeast cells by supported sol – gel entrapment for efficient acyloin condensation

    Nagy-Győr L., Farkas E., Lăcătuș M., Tóth G., Incze D., Hornyánszky G., Bódai V., Paizs C., Poppe L., Balogh-Weiser D.
    Periodica Polytechnica Chemical Engineering (2020) 64(2): 153-161
    DOI: 10.3311/PPch.14645

  12. Effcient and stable magnetic chitosan-lipase B from candida antarctica bioconjugates in the enzymatic kinetic resolution of racemic heteroarylethanols

    Spelmezan C.G., Bencze L.C., Katona G., Irimie F.D., Paizs C., Tos M.I.
    Molecules (2020) 25(2): 153-161
    DOI: 10.3390/molecules25020350

  13. Efficient biodiesel production catalyzed by nanobioconjugate of lipase from pseudomonas fluorescens

    Bartha-Vári J.-H., Moisă M.E., Bencze L.C., Irimie F.-D., Paizs C., Toșa M.I.
    Molecules (2020) 25(3): 153-161
    DOI: 10.3390/molecules25030651