@article{MTMT:34830192,
	title = {Immobilization of human tyrosine hydroxylase onto magnetic nanoparticles – A novel formulation of a therapeutic enzyme},
	url = {https://m2.mtmt.hu/api/publication/34830192},
	author = {Molnár, Zsófia Klára and Koplányi, Gábor and Farkas, Réka and Péli, Noémi and Kenéz, Balázs and Decsi, Balázs and Katona, Gábor and Balogh, György Tibor and Vértessy, Beáta (Grolmuszné) and Balogh Weiser, Diána},
	doi = {10.1016/j.ijbiomac.2024.131939},
	journal-iso = {INT J BIOL MACROMOL},
	journal = {INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES},
	volume = {268},
	unique-id = {34830192},
	issn = {0141-8130},
	abstract = {Human tyrosine hydroxylase (hTH) has key role in the production of catecholamine neurotransmitters. The structure, function and regulation of hTH has been extensively researched area and the possibility of enzyme replacement therapy (ERT) involving hTH through nanocarriers has been raised as well. However, our understanding on how hTH may interact with nanocarriers is still lacking. In this work, we attempted to investigate the immobilization of hTH on magnetic nanoparticles (MNPs) with various surface linkers in quantitative and mechanistic detail. Our results showed that the activity of hTH was retained after immobilization via secondary and covalent interactions as well. The colloidal stability of hTH could be also enhanced proved by Dynamic light scattering and Zeta potential analysis and a homogenous enzyme layer could be achieved, which was investigated by Raman mapping. The covalent attachment of hTH on MNPs via aldehyde or epoxy linkers provide irreversible immobilization and 38.1 % and 16.5 % recovery (ER). The hTH-MNPs catalyst had 25 % ER in average in simulated nasal electrolyte solution (SNES). This outcome highlights the relevance of immobilization applying MNPs as a potential formulation tool of sensitive therapeutic enzymes offering new opportunities for ERT related to neurodegenerative disorders. © 2024 The Author(s)},
	year = {2024},
	eissn = {1879-0003},
	orcid-numbers = {Koplányi, Gábor/0000-0002-3791-1057; Katona, Gábor/0000-0003-1564-4813; Balogh, György Tibor/0000-0003-3347-1880; Balogh Weiser, Diána/0000-0002-9957-1203}
}

@article{MTMT:34522222,
	title = {Discovery and biocatalytic characterization of opine dehydrogenases by metagenome mining},
	url = {https://m2.mtmt.hu/api/publication/34522222},
	author = {Telek, András and Molnár, Zsófia Klára and Takács, Kristóf and Varga, Bálint and Grolmusz, Vince and Tasnádi, Gábor and Vértessy, Beáta (Grolmuszné)},
	doi = {10.1007/s00253-023-12871-z},
	journal-iso = {APPL MICROBIOL BIOT},
	journal = {APPLIED MICROBIOLOGY AND BIOTECHNOLOGY},
	volume = {108},
	unique-id = {34522222},
	issn = {0175-7598},
	year = {2024},
	eissn = {1432-0614},
	orcid-numbers = {Telek, András/0000-0002-1909-8410; Molnár, Zsófia Klára/0000-0002-9552-7061; Grolmusz, Vince/0000-0001-9456-8876; Tasnádi, Gábor/0000-0002-4877-1889}
}

@article{MTMT:34039046,
	title = {Opine dehydrogenases, an underexplored enzyme family for the enzymatic synthesis of chiral amines},
	url = {https://m2.mtmt.hu/api/publication/34039046},
	author = {Telek, András and Molnár, Zsófia Klára and Vértessy, Beáta (Grolmuszné) and Tasnádi, Gábor},
	doi = {10.1002/bit.28469},
	journal-iso = {BIOTECHNOL BIOENG},
	journal = {BIOTECHNOLOGY AND BIOENGINEERING},
	volume = {120},
	unique-id = {34039046},
	issn = {0006-3592},
	year = {2023},
	eissn = {1097-0290},
	pages = {2793-2808},
	orcid-numbers = {Telek, András/0000-0002-1909-8410; Tasnádi, Gábor/0000-0002-4877-1889}
}

@article{MTMT:33574611,
	title = {Novel Approach for the Isolation and Immobilization of a Recombinant Transaminase. Applying an Advanced Nanocomposite System},
	url = {https://m2.mtmt.hu/api/publication/33574611},
	author = {Koplányi, Gábor and Bell, Evelin and Molnár, Zsófia Klára and Katona, Gábor and Neumann, Péter Lajos and Ender, Ferenc and Balogh, György Tibor and Žnidaršič-Plazl, Polona and Poppe, László and Balogh Weiser, Diána},
	doi = {10.1002/cbic.202200713},
	journal-iso = {CHEMBIOCHEM},
	journal = {CHEMBIOCHEM},
	volume = {24},
	unique-id = {33574611},
	issn = {1439-4227},
	year = {2023},
	eissn = {1439-7633},
	orcid-numbers = {Koplányi, Gábor/0000-0002-3791-1057; Katona, Gábor/0000-0003-1564-4813; Neumann, Péter Lajos/0000-0002-2881-5733; Ender, Ferenc/0000-0003-3800-5707; Balogh, György Tibor/0000-0003-3347-1880; Poppe, László/0000-0002-8358-1378; Balogh Weiser, Diána/0000-0002-9957-1203}
}

@article{MTMT:33077292,
	title = {Diverging enantiopreferences: insights into the phenylalanine aminomutase mechanism and evolution},
	url = {https://m2.mtmt.hu/api/publication/33077292},
	author = {Molnár, Zsófia Klára and Poppe, László and Vértessy, Beáta (Grolmuszné)},
	journal-iso = {FEBS OPEN BIO},
	journal = {FEBS OPEN BIO},
	volume = {12},
	unique-id = {33077292},
	issn = {2211-5463},
	year = {2022},
	eissn = {2211-5463},
	pages = {245-246},
	orcid-numbers = {Poppe, László/0000-0002-8358-1378}
}

@article{MTMT:32650829,
	title = {Immobilization of the Aspartate Ammonia-Lyase from Pseudomonas fluorescens R124 on Magnetic Nanoparticles: Characterization and Kinetics},
	url = {https://m2.mtmt.hu/api/publication/32650829},
	author = {Csuka, Pál and Molnár, Zsófia Klára and Tóth, Veronika and Imarah, Ali O. and Balogh Weiser, Diána and Vértessy, Beáta (Grolmuszné) and Poppe, László},
	doi = {10.1002/cbic.202100708},
	journal-iso = {CHEMBIOCHEM},
	journal = {CHEMBIOCHEM},
	volume = {23},
	unique-id = {32650829},
	issn = {1439-4227},
	abstract = {Aspartate ammonia-lyases (AALs) catalyze the non-oxidative elimination of ammonia from l-aspartate to give fumarate and ammonia. In this work the AAL coding gene from Pseudomonas fluorescens R124 was identified, isolated, and cloned into the pET-15b expression vector and expressed in E. coli. The purified enzyme (PfAAL) showed optimal activity at pH 8.8, Michaelis-Menten kinetics in the ammonia elimination from l-aspartate, and no strong dependence on divalent metal ions for its activity. The purified PfAAL was covalently immobilized on epoxy-functionalized magnetic nanoparticles (MNP), and effective kinetics of the immobilized PfAAL-MNP was compared to the native solution form. Glycerol addition significantly enhanced the storability of PfAAL-MNP. Inhibiting effect of the growing viscosity (modulated by addition of glycerol or glucose) on the enzymatic activity was observed for the native and immobilized form of PfAAL, as previously described for other free enzymes. The storage stability and recyclability of PfAAL-MNP is promising for further biocatalytic applications. © 2022 The Authors. ChemBioChem published by Wiley-VCH GmbH},
	year = {2022},
	eissn = {1439-7633},
	orcid-numbers = {Balogh Weiser, Diána/0000-0002-9957-1203; Poppe, László/0000-0002-8358-1378}
}

@mastersthesis{MTMT:32522108,
	title = {Rekombináns ammónia-liázok és transzaminázok mint sztereoszelektív biokatalizátorok},
	url = {https://m2.mtmt.hu/api/publication/32522108},
	author = {Molnár, Zsófia Klára},
	publisher = {Budapest University of Technology and Economics},
	unique-id = {32522108},
	year = {2021}
}

@article{MTMT:32242806,
	title = {Entrapment of Phenylalanine Ammonia-Lyase in Nanofibrous Polylactic Acid Matrices by Emulsion Electrospinning},
	url = {https://m2.mtmt.hu/api/publication/32242806},
	author = {Koplányi, Gábor and Bell, Evelin and Molnár, Zsófia Klára and Tóth, Gergő Dániel and Józó, Muriel and Szilágyi, András Ferenc and Ender, Ferenc and Pukánszky, Béla and Vértessy, Beáta (Grolmuszné) and Poppe, László and Balogh Weiser, Diána},
	doi = {10.3390/catal11101149},
	journal-iso = {CATALYSTS},
	journal = {CATALYSTS},
	volume = {11},
	unique-id = {32242806},
	year = {2021},
	eissn = {2073-4344},
	orcid-numbers = {Koplányi, Gábor/0000-0002-3791-1057; Szilágyi, András Ferenc/0000-0001-6898-1755; Ender, Ferenc/0000-0003-3800-5707; Poppe, László/0000-0002-8358-1378; Balogh Weiser, Diána/0000-0002-9957-1203}
}

@article{MTMT:32083731,
	title = {Immobilization of Phenylalanine Ammonia-lyase via EDTA Based Metal Chelate Complexes - Optimization and Prospects},
	url = {https://m2.mtmt.hu/api/publication/32083731},
	author = {Bell, Evelin and Kovacs, Norbert Krisztian and Alacs, Balint and Molnár, Zsófia Klára and Hornyánszky, Gábor},
	doi = {10.3311/PPch.17891},
	journal-iso = {PERIOD POLYTECH CHEM ENG},
	journal = {PERIODICA POLYTECHNICA-CHEMICAL ENGINEERING},
	volume = {65},
	unique-id = {32083731},
	issn = {0324-5853},
	abstract = {Immobilized metal ion affinity chromatography principles were applied for selective immobilization of recombinant polyhistidine tag fused phenylalanine ammonia-lyase from parsley (PcPAL) on porous polymeric support with aminoaikyl moieties modified with an EDTA dianhydride (EDTADa)-derived chelator and charged with transition metal ions. Out of the five investigated metal ions - Fe3+, Co2+, NP2+, Cu2+, Zn2+- the best biocatalytic activity of PcPAL was achieved when the enzyme was immobilized on the Co2+ ion-charged support (31.8 +/- 1.2 U/g). To explore the features this PcPAL obtained by selective immobilization, the thermostability and reusability of this PAL biocatalyst were investigated. To maximize the activity of the immobilized PcPAL the surface functionalization of the aminoalkylated polymeric carrier was fine-tuned with using glycidol as a thinning group beside EDTADa. The maximal activity yield (Y-A=103 %) was earned when the EDTADa and glycidol were used in 1 to 24 ratio. The reversibility of the immobilization method allowed the development of a support regeneration protocol which enables easy reuse of the functionalized support in case of enzyme inactivation.},
	keywords = {ACID; STABILIZATION; KINETIC RESOLUTION; SILICA-GEL; Covalent immobilization; IMAC; REVERSIBLE IMMOBILIZATION; AFFINITY-CHROMATOGRAPHY; selective enzyme immobilization; PROTEIN-PURIFICATION; D-HYDANTOINASE},
	year = {2021},
	eissn = {1587-3765},
	pages = {308-319}
}

@article{MTMT:32071510,
	title = {Characterization of Yeast Strains with Ketoreductase Activity for Bioreduction of Ketones},
	url = {https://m2.mtmt.hu/api/publication/32071510},
	author = {Csuka, Pál and Nagy-Győr, László and Molnár, Zsófia Klára and Paizs, Csaba and Erdélyiné Bódai, Viktória and Poppe, László},
	doi = {10.3311/PPch.17429},
	journal-iso = {PERIOD POLYTECH CHEM ENG},
	journal = {PERIODICA POLYTECHNICA-CHEMICAL ENGINEERING},
	volume = {65},
	unique-id = {32071510},
	issn = {0324-5853},
	year = {2021},
	eissn = {1587-3765},
	pages = {299-307},
	orcid-numbers = {Paizs, Csaba/0000-0002-7403-7098; Poppe, László/0000-0002-8358-1378}
}