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001-es BibID:	BIBFORM115504
035-os BibID:	(WoS)001088971700003 (Scopus)85174404537
Első szerző:	Bodnár Magdolna
Cím:	Synthesis of Galacto-oligosaccharides in Milk by Using Bifidobacterium bifidum β-galactosidases (Saphera 2600L and Nola Fit 5500) Immobilized on Chitosan Beads / Bodnár Magdolna, Fazekas Erika, Nagy Tibor, Miltner Noémi, Kalló Gergő, Kerekes Krisztina, Prépost Eszter, Mótyán János András
Dátum:	2023
ISSN:	1935-5130 1935-5149
Megjegyzések:	The lactose intolerance-as a limiting factor for dairy milk consumption-has a high prevalence worldwide. Dairy milk and milk-derived products are major sources of multiple inorganic compounds and nutrients and thus are considered to be functional foods. beta-galactosidases are able to hydrolyze lactose and are therefore widely applied for the production of lactose-free products. In addition, they are capable of the synthesis of galacto-oligosaccharides (GOSs); thus, the dairy industry has a special interest in applying them for the enrichment of dairy products with prebiotic GOSs. In this work, we studied two commercially available beta-galactosidase products: Saphera 2600L and Nola Fit 5500. Both enzyme solutions contain a recombinant beta-galactosidase of Bifidobacterium bifidum and have already been authorized for food industrial application, but the information about their hydrolytic and/or synthetic activities is only limited. After immobilization on chitosan beads, the enzymes were used for lactose hydrolysis and simultaneous synthesis of GOSs, by performing the reactions in pasteurized milk (skim milk). Both immobilized beta-galactosidase exhibited elevated lactose hydrolysis (vmax increased from similar to 1 to similar to 4 mM/min) and GOS synthesis as compared to the free enzymes. The enzyme-coated beads were efficiently re-used at least 15 cycles; the residual lactose concentration was < 2 mg/ml after each cycle. After treatment, GOSs were present in <= 9% of the total sugar content, indicating that the prepared low-lactose milks were enriched in prebiotic GOSs. The application of immobilized Saphera 2600L and Nola Fit 5500 beta-galactosidases may be implemented for the large-scale production of GOS-enriched low-lactose milk.
Tárgyszavak:	Agrártudományok Élelmiszertudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Lactose-free milk GOS-enriched milk Enzyme immobilization Chitosan Lactase β-galactosidase Transgalactosylation Galacto-oligosaccharide GOS
Megjelenés:	Food and Bioprocess Technology. - [Epub ahead of print] (2023). -
További szerzők:	Fazekas Erika (1985-) (kémikus) Nagy Tibor (1988-) (vegyész) Miltner Noémi (1990-) (molekuláris biológus) Kalló Gergő (1989-) (molekuláris biológus) Kerekes Krisztina Prépost Eszter Mótyán János András (1981-) (biokémikus, molekuláris biológus)
Pályázati támogatás:	2019-1.1.1-PIACI-KFI-2019-00109 Egyéb FK-132385 OTKA GINOP-2.3.3-15-2016-00020 GINOP
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001-es BibID:	BIBFORM091513
035-os BibID:	(cikkazonosító)1648 (scopus)85100462177 (wos)000623909700001
Első szerző:	Borbély Adina
Cím:	Structural Characterization of Daunomycin-Peptide Conjugates by Various Tandem Mass Spectrometric Techniques / Adina Borbély, Lilla Pethő, Ildikó Szabó, Mohammed Al-Majidi, Arnold Steckel, Tibor Nagy, Sándor Kéki, Gergő Kalló, Éva Csősz, Gábor Mező, Gitta Schlosser
Dátum:	2021
ISSN:	1661-6596 1422-0067
Megjegyzések:	The use of peptide-drug conjugates has generated wide interest as targeted antitumor therapeutics. The anthracycline antibiotic, daunomycin, is a widely used anticancer agent and it is often conjugated to different tumor homing peptides. However, comprehensive analytical characterization of these conjugates via tandem mass spectrometry (MS/MS) is challenging due to the lability of the O-glycosidic bond and the appearance of MS/MS fragment ions with little structural information. Therefore, we aimed to investigate the optimal fragmentation conditions that suppress the prevalent dissociation of the anthracycline drug and provide good sequence coverage. In this study, we comprehensively compared the performance of common fragmentation techniques, such as higher energy collisional dissociation (HCD), electron transfer dissociation (ETD), electron-transfer higher energy collisional dissociation (EThcD) and matrix-assisted laser desorption/ionization-tandem time-of-flight (MALDI-TOF/TOF) activation methods for the structural identification of synthetic daunomycin-peptide conjugates by high-resolution tandem mass spectrometry. Our results showed that peptide backbone fragmentation was inhibited by applying electron-based dissociation methods to conjugates, most possibly due to the "electron predator" effect of the daunomycin. We found that efficient HCD fragmentation was largely influenced by several factors, such as amino acid sequences, charge states and HCD energy. High energy HCD and MALDI-TOF/TOF combined with collision induced dissociation (CID) mode are the methods of choice to unambiguously assign the sequence, localize different conjugation sites and differentiate conjugate isomers.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk MALDI anthracyclines bioconjugates collision-induced dissociation electron predator high resolution mass spectrometry
Megjelenés:	International Journal Of Molecular Sciences. - 22 : 4 (2021), p. 1-15. -
További szerzők:	Pethő Lilla Szabó Ildikó Al-Majidi, Mohammed Steckel Arnold Nagy Tibor (1988-) (vegyész) Kéki Sándor (1964-) (polimer kémikus) Kalló Gergő (1989-) (molekuláris biológus) Csősz Éva (1977-) (biokémikus, molekuláris biológus) Mező Gábor (1959-) (vegyész) Schlosser Gitta
Pályázati támogatás:	NVKP_16-1-2016-0036 Egyéb Lendület Momentum Program Egyéb VEKOP- 387 2.3.3-15-2017-00020 Egyéb GINOP-2.3.3-15-2016-00020 GINOP GINOP-2.3.3-15-2016-00021 GINOP
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001-es BibID:	BIBFORM108752
035-os BibID:	(cikkazonosító)3236 (Scopus)85148962397 (WoS)000938549700001
Első szerző:	Miltner Noémi (molekuláris biológus)
Cím:	Identification of SARS-CoV-2 Main Protease (Mpro) Cleavage Sites Using Two-Dimensional Electrophoresis and In Silico Cleavage Site Prediction / Noémi Miltner, Gergő Kalló, Éva Csősz, Márió Miczi, Tibor Nagy, Mohamed Mahdi, János András Mótyán, József Tőzsér
Dátum:	2023
ISSN:	1422-0067
Megjegyzések:	The main protease (Mpro) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) plays a crucial role in its life cycle. The Mpro-mediated limited proteolysis of the viral polyproteins is necessary for the replication of the virus, and cleavage of the host proteins of the infected cells may also contribute to viral pathogenesis, such as evading the immune responses or triggering cell toxicity. Therefore, the identification of host substrates of the viral protease is of special interest. To identify cleavage sites in cellular substrates of SARS-CoV-2 Mpro, we determined changes in the HEK293T cellular proteome upon expression of the Mpro using two-dimensional gel electrophoresis. The candidate cellular substrates of Mpro were identified by mass spectrometry, and then potential cleavage sites were predicted in silico using NetCorona 1.0 and 3CLP web servers. The existence of the predicted cleavage sites was investigated by in vitro cleavage reactions using recombinant protein substrates containing the candidate target sequences, followed by the determination of cleavage positions using mass spectrometry. Unknown and previously described SARS-CoV-2 Mpro cleavage sites and cellular substrates were also identified. Identification of target sequences is important to understand the specificity of the enzyme, as well as aiding the improvement and development of computational methods for cleavage site prediction.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk coronavirus SARS-CoV-2 main protease Mpro COVID-19 two-dimensional gel electrophoresis cleavage site identification cleavage site prediction protease host protein cleavage specificity
Megjelenés:	International Journal Of Molecular Sciences. - 24 : 4 (2023), p. 1-19. -
További szerzők:	Kalló Gergő (1989-) (molekuláris biológus) Csősz Éva (1977-) (biokémikus, molekuláris biológus) Miczi Márió Nagy Tibor (1988-) (vegyész) Mahdi, Mohamed (1979-) (orvos, tudományos segédmunkatárs) Mótyán János András (1981-) (biokémikus, molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:	GINOP-2.3.3-15-2016-00020 GINOP GINOP-2.3.3-15-2016-00021 GINOP
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