Results
ü
Highly stable and active biocatalysts were
developed through covalent site-specific immobilization of PcPAL
variants (with Cys residues introduced at the
enzyme’s surface by site-directed mutagenesis) onto maleimide-functionalized
amino-single-walled carbon nanotubes
ü
Efficient procedures for the enzymatic
synthesis of highly valuable l-phenylalanines in batch and continuous-flow systems were
developed by the use of novel site-specifically immobilized biocatalysts
ü Phenylalanine
ammonia-lyases from different sources were tailored through rational
modification of the hydrophobic binding pocket for the synthesis of a variety
of unnatural d- and l-phenylalanines
ü A
general rational design strategy for substrate-tailored PALs was proposed
Publications & conferences
1. Krisztina Boros, Mădălina Elena
Moisă, Levente Csaba Nagy, Csaba Paizs, Monica Ioana Toşa, László
Csaba Bencze, Robust, site-specifically immobilized phenylalanine
ammonia-lyases for the enantioselective ammonia addition of cinnamic acids, Catal. Sci. Technol. 2021, 11, 5553-5563, DOI: 10.1039/d1cy00195g.
2.
Souad Diana Tork, Mădălina
Elena Moisă, Lilla Cserepes,
Alina Filip, Levente Csaba Nagy, Florin Dan Irimie, László Csaba Bencze, Towards a general approach for tailoring the
hydrophobic binding site of phenylalanine ammonia‑lyases, Sci. Rep. 2022, 12, 10606,
DOI:10.1038/s41598-022-14585-0.
3. Mădălina Elena Moisă, Judith-Hajnal Bartha-Vári,
László-Csaba Bencze, Florin Dan Irimie,
Csaba Paizs, Monica Ioana Toșa, Site-specifically immobilized phenylalanine
ammonia lyases for continuous flow processes, The 13the
International Symposium of the Romanian Catalysis Society RomCat2022, Băile Govora, 20-24 June 2022 – poster
presentation