TY - JOUR AU - Telek, András AU - Molnár, Zsófia Klára AU - Takács, Kristóf AU - Varga, Bálint AU - Grolmusz, Vince AU - Tasnádi, Gábor AU - Vértessy, Beáta (Grolmuszné) TI - Discovery and biocatalytic characterization of opine dehydrogenases by metagenome mining JF - APPLIED MICROBIOLOGY AND BIOTECHNOLOGY J2 - APPL MICROBIOL BIOT VL - 108 PY - 2024 IS - 1 PG - 16 SN - 0175-7598 DO - 10.1007/s00253-023-12871-z UR - https://m2.mtmt.hu/api/publication/34522222 ID - 34522222 N1 - Department of Applied Biotechnology, Budapest University of Technology and Economics, Budapest, Hungary Servier Research Institute of Medicinal Chemistry, Budapest, Hungary Institute of Molecular Life Sciences, Research Centre for Natural Sciences, HUN-REN, Budapest, Hungary Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Budapest, Hungary PIT Bioinformatics Group, Institute of Mathematics, Eötvös University, Budapest, Hungary Export Date: 22 February 2024 CODEN: AMBID Correspondence Address: Vértessy, B.G.; Department of Applied Biotechnology, Hungary; email: vertessy.beata@ttk.hu Correspondence Address: Tasnádi, G.; Servier Research Institute of Medicinal ChemistryHungary; email: gabor.tasnadi@servier.com LA - English DB - MTMT ER - TY - JOUR AU - Telek, András AU - Molnár, Zsófia Klára AU - Vértessy, Beáta (Grolmuszné) AU - Tasnádi, Gábor TI - Opine dehydrogenases, an underexplored enzyme family for the enzymatic synthesis of chiral amines JF - BIOTECHNOLOGY AND BIOENGINEERING J2 - BIOTECHNOL BIOENG VL - 120 PY - 2023 IS - 10 SP - 2793 EP - 2808 PG - 16 SN - 0006-3592 DO - 10.1002/bit.28469 UR - https://m2.mtmt.hu/api/publication/34039046 ID - 34039046 N1 - Export Date: 29 June 2023 CODEN: BIBIA Correspondence Address: Vértessy, B.G.; Department of Applied Biotechnology, Szt. Gellért tér 4, Hungary; email: vertessy.beata@vbk.bme.hu Correspondence Address: Tasnádi, G.; Servier Research Institute of Medicinal ChemistryHungary; email: gabor.tasnadi@servier.com LA - English DB - MTMT ER - TY - JOUR AU - Koplányi, Gábor AU - Bell, Evelin AU - Molnár, Zsófia Klára AU - Katona, Gábor AU - Neumann, Péter Lajos AU - Ender, Ferenc AU - Balogh, György Tibor AU - Žnidaršič-Plazl, Polona AU - Poppe, László AU - Balogh Weiser, Diána TI - Novel Approach for the Isolation and Immobilization of a Recombinant Transaminase. Applying an Advanced Nanocomposite System TS - Applying an Advanced Nanocomposite System JF - CHEMBIOCHEM J2 - CHEMBIOCHEM VL - 24 PY - 2023 IS - 7 PG - 11 SN - 1439-4227 DO - 10.1002/cbic.202200713 UR - https://m2.mtmt.hu/api/publication/33574611 ID - 33574611 LA - English DB - MTMT ER - TY - JOUR AU - Molnár, Zsófia Klára AU - Poppe, László AU - Vértessy, Beáta (Grolmuszné) TI - Diverging enantiopreferences: insights into the phenylalanine aminomutase mechanism and evolution JF - FEBS OPEN BIO J2 - FEBS OPEN BIO VL - 12 PY - 2022 IS - S1 SP - 245 EP - 246 PG - 2 SN - 2211-5463 UR - https://m2.mtmt.hu/api/publication/33077292 ID - 33077292 LA - English DB - MTMT ER - TY - JOUR AU - Csuka, Pál AU - Molnár, Zsófia Klára AU - Tóth, Veronika AU - Imarah, Ali O. AU - Balogh Weiser, Diána AU - Vértessy, Beáta (Grolmuszné) AU - Poppe, László TI - Immobilization of the Aspartate Ammonia-Lyase from Pseudomonas fluorescens R124 on Magnetic Nanoparticles: Characterization and Kinetics JF - CHEMBIOCHEM J2 - CHEMBIOCHEM VL - 23 PY - 2022 IS - 7 PG - 9 SN - 1439-4227 DO - 10.1002/cbic.202100708 UR - https://m2.mtmt.hu/api/publication/32650829 ID - 32650829 N1 - Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, 1111, Hungary Institute of Enzymology, ELKH Research Center of Natural Sciences, Magyar tudósok krt. 2, Budapest, 1117, Hungary Department of Physical Chemistry and Materials Science, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, 1111, Hungary Department of Applied Biotechnology and Food Science, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, 1111, Hungary Biocatalysis and Biotransformation Research Center, Faculty of Chemistry and Chemical Engineering, Babeş-Bolyai University of Cluj-Napoca, Arany János Str. 11, Cluj-Napoca, 400028, Romania Export Date: 6 April 2022 CODEN: CBCHF Correspondence Address: Poppe, L.; Department of Organic Chemistry and Technology, Műegyetem rkp. 3, Hungary; email: poppe.laszlo@vbk.bme.hu Funding details: 103413, NKP‐2018‐1.2.1‐NKP‐2018‐00005, P37_273 Funding details: National Authority for Scientific Research and Innovation, ANCSI Funding details: Magyar Tudományos Akadémia, MTA Funding details: European Regional Development Fund, ERDF Funding details: Richter Gedeon Talentum Alapítvány Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, NKFIA Funding details: Innovációs és Technológiai Minisztérium Funding details: National Research, Development and Innovation Office, FK‐137582, PD‐131467 Funding text 1: The research reported in this paper is part of project no. TKP2021‐EGA‐02, implemented with the support provided by the Ministry for Innovation and Technology of Hungary from the National Research, Development and Innovation Fund, financed under the TKP2021 funding scheme. The National Research, Development and Innovation Office (Budapest, Hungary) is acknowledged for funding (L. P.: SNN‐125637, D. B. W.: PD‐131467, FK‐137582 and L. P., B. G. V.: NRDI Office NKP‐2018‐1.2.1‐NKP‐2018‐00005). L. P. thanks the financial funding for project NEMSyB, ID P37_273, Cod MySMIS 103413 [funded by the Romanian Ministry for European Funds, through the National Authority for Scientific Research and Innovation (ANCSI) and co‐funded by the European Regional Development Fund, Competitiveness Operational Program 2014–2020 (POC)] is also acknowledged. The authors also acknowledge the Gedeon Richter Talentum Foundation for the PhD fellowship of Z. M. This study was also supported by the ÚNKP‐21‐4 (Z. M.) and ÚNKP‐21‐5 (D. B. W.) New National Excellence Program of the Ministry for Innovation and Technology from the source of the national research, development, and innovation fund and by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences (D. B. W.). AB - 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 LA - English DB - MTMT ER - TY - THES AU - Molnár, Zsófia Klára TI - Rekombináns ammónia-liázok és transzaminázok mint sztereoszelektív biokatalizátorok PB - Budapesti Műszaki és Gazdaságtudományi Egyetem PY - 2021 SP - 108 UR - https://m2.mtmt.hu/api/publication/32522108 ID - 32522108 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Koplányi, Gábor AU - Bell, Evelin AU - Molnár, Zsófia Klára AU - Tóth, Gergő Dániel AU - Józó, Muriel AU - Szilágyi, András Ferenc AU - Ender, Ferenc AU - Pukánszky, Béla AU - Vértessy, Beáta (Grolmuszné) AU - Poppe, László AU - Balogh Weiser, Diána TI - Entrapment of Phenylalanine Ammonia-Lyase in Nanofibrous Polylactic Acid Matrices by Emulsion Electrospinning JF - CATALYSTS J2 - CATALYSTS VL - 11 PY - 2021 IS - 10 PG - 14 SN - 2073-4344 DO - 10.3390/catal11101149 UR - https://m2.mtmt.hu/api/publication/32242806 ID - 32242806 N1 - Export Date: 26 October 2021 LA - English DB - MTMT ER - TY - JOUR AU - Bell, Evelin AU - Kovacs, Norbert Krisztian AU - Alacs, Balint AU - Molnár, Zsófia Klára AU - Hornyánszky, Gábor TI - Immobilization of Phenylalanine Ammonia-lyase via EDTA Based Metal Chelate Complexes - Optimization and Prospects JF - PERIODICA POLYTECHNICA-CHEMICAL ENGINEERING J2 - PERIOD POLYTECH CHEM ENG VL - 65 PY - 2021 IS - 3 SP - 308 EP - 319 PG - 12 SN - 0324-5853 DO - 10.3311/PPch.17891 UR - https://m2.mtmt.hu/api/publication/32083731 ID - 32083731 N1 - Funding Agency and Grant Number: NRDI Fund [project (TKP2020 IES)] under Ministry for Innovation and Technology [BME-IE-BIO]; [SNN-125637] Funding text: The research reported in this paper and carried out at BME has been supported by the NRDI Fund [project (TKP2020 IES, Grant No. BME-IE-BIO) based on the charter of bolster issued by the NRDI Office under the auspices of the Ministry for Innovation and Technology; and project (SNN-125637)]. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Csuka, Pál AU - Nagy-Győr, László AU - Molnár, Zsófia Klára AU - Paizs, Csaba AU - Erdélyiné Bódai, Viktória AU - Poppe, László TI - Characterization of Yeast Strains with Ketoreductase Activity for Bioreduction of Ketones JF - PERIODICA POLYTECHNICA-CHEMICAL ENGINEERING J2 - PERIOD POLYTECH CHEM ENG VL - 65 PY - 2021 IS - 3 SP - 299 EP - 307 PG - 9 SN - 0324-5853 DO - 10.3311/PPch.17429 UR - https://m2.mtmt.hu/api/publication/32071510 ID - 32071510 LA - English DB - MTMT ER - TY - JOUR AU - Imarah, Ali O. AU - Csuka, Pál AU - Bataa, Naran AU - Decsi, Balázs AU - Bell, Evelin AU - Molnár, Zsófia Klára AU - Balogh Weiser, Diána AU - Poppe, László TI - Magnetically Agitated Nanoparticle-Based Batch Reactors for Biocatalysis with Immobilized Aspartate Ammonia-Lyase JF - CATALYSTS J2 - CATALYSTS VL - 11 PY - 2021 IS - 4 PG - 13 SN - 2073-4344 DO - 10.3390/catal11040483 UR - https://m2.mtmt.hu/api/publication/31959087 ID - 31959087 N1 - Funding Agency and Grant Number: National Research, Development and Innovation Office (Budapest, Hungary) [TKP2020 IES, BME-IE-BIO]; OTKAOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [SNN-125637, PD-131467] Funding text: This research was funded by the National Research, Development and Innovation Office (Budapest, Hungary), grant numbers TKP2020 IES, Grant No. BME-IE-BIO, and OTKA, SNN-125637 and PD-131467. Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, H-1111, Hungary Chemical Engineering Department, College of Engineering, University of Babylon, Hilla Babylon, 5100, Iraq Fermentia Microbiological Ltd, Berlini út 47-49, Budapest, H-1045, Hungary Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Science, Magyar tudósok körútja 2, Budapest, H-1117, Hungary Department of Phsysical Chemistry and Materials Science, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, H-1111, Hungary SynBiocat Ltd, Szilasliget u 3, Budapest, H-1172, Hungary Biocatalysis and Biotransformation Research Center, Faculty of Chemistry and Chemical Engineering, Babeş-Bolyai University of Cluj-Napoca, Arany János Str. 11, Cluj-Napoca, RO-400028, Romania Export Date: 13 May 2021 Correspondence Address: Poppe, L.; Department of Organic Chemistry and Technology, Műegyetem rkp. 3, Hungary; email: poppe.laszlo@vbk.bme.hu Correspondence Address: Poppe, L.; SynBiocat Ltd, Szilasliget u 3, Hungary; email: poppe.laszlo@vbk.bme.hu Correspondence Address: Poppe, L.; Biocatalysis and Biotransformation Research Center, Arany János Str. 11, Romania; email: poppe.laszlo@vbk.bme.hu Funding details: Hungarian Scientific Research Fund, OTKA, PD-131467, SNN-125637 Funding details: National Research, Development and Innovation Office Funding text 1: Funding: This research was funded by the National Research, Development and Innovation Office (Budapest, Hungary), grant numbers TKP2020 IES, Grant No. BME-IE-BIO, and OTKA, SNN-125637 and PD-131467. Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, H-1111, Hungary Chemical Engineering Department, College of Engineering, University of Babylon, Hilla Babylon, 5100, Iraq Fermentia Microbiological Ltd, Berlini út 47-49, Budapest, H-1045, Hungary Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Science, Magyar tudósok körútja 2, Budapest, H-1117, Hungary Department of Phsysical Chemistry and Materials Science, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, H-1111, Hungary SynBiocat Ltd, Szilasliget u 3, Budapest, H-1172, Hungary Biocatalysis and Biotransformation Research Center, Faculty of Chemistry and Chemical Engineering, Babeş-Bolyai University of Cluj-Napoca, Arany János Str. 11, Cluj-Napoca, RO-400028, Romania Export Date: 14 May 2021 Correspondence Address: Poppe, L.; Department of Organic Chemistry and Technology, Műegyetem rkp. 3, Hungary; email: poppe.laszlo@vbk.bme.hu Correspondence Address: Poppe, L.; SynBiocat Ltd, Szilasliget u 3, Hungary; email: poppe.laszlo@vbk.bme.hu Correspondence Address: Poppe, L.; Biocatalysis and Biotransformation Research Center, Arany János Str. 11, Romania; email: poppe.laszlo@vbk.bme.hu Funding details: Hungarian Scientific Research Fund, OTKA, PD-131467, SNN-125637 Funding details: National Research, Development and Innovation Office Funding text 1: Funding: This research was funded by the National Research, Development and Innovation Office (Budapest, Hungary), grant numbers TKP2020 IES, Grant No. BME-IE-BIO, and OTKA, SNN-125637 and PD-131467. AB - In this study, we investigated the influence of different modes of magnetic mixing on effective enzyme activity of aspartate ammonia-lyase from Pseudomonas fluorescens immobilized onto epoxy-functionalized magnetic nanoparticles by covalent binding (AAL-MNP). The effective specific enzyme activity of AAL-MNPs in traditional shake vial method was compared to the specific activity of the MNP-based biocatalyst in two devices designed for magnetic agitation. The first device agitated the AAL-MNPs by moving two permanent magnets at two opposite sides of a vial in x-axis direction (being perpendicular to the y-axis of the vial); the second device unsettled the MNP biocatalyst by rotating the two permanent magnets around the y-axis of the vial. In a traditional shake vial, the substrate and biocatalyst move in the same direction with the same pattern. In magnetic agitation modes, the MNPs responded differently to the external magnetic field of two permanent magnets. In the axial agitation mode, MNPs formed a moving cloud inside the vial, whereas in the rotating agitation mode, they formed a ring. Especially, the rotating agitation of the MNPs generated small fluid flow inside the vial enabling the mixing of the reaction mixture, leading to enhanced effective activity of AAL-MNPs compared to shake vial agitation. LA - English DB - MTMT ER -