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1.

001-es BibID:BIBFORM115504
035-os BibID:(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. ?-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 ?-galactosidase products: Saphera 2600L and Nola Fit 5500. Both enzyme solutions contain a recombinant ?-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 ?-galactosidase exhibited elevated lactose hydrolysis (vmax increased from?~?1 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 ?-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
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM082814
035-os BibID:(cikkazonosító)e0227062 (WOS)000534341100013 (Scopus)85077691494
Első szerző:Gazda Lívia Diána
Cím:Biochemical characterization of Ty1 retrotransposon protease / Lívia Diána Gazda, Krisztina Joóné Matúz, Tibor Nagy, János András Mótyán, József Tőzsér
Dátum:2020
ISSN:1932-6203
Megjegyzések:Ty1 is one of the many transposons in the budding yeast Saccharomyces cerevisiae. The life-cycle of Ty1 shows numerous similarities with that of retroviruses, e.g. the initially synthesized polyprotein precursor undergoes proteolytic processing by the protease. The retroviral proteases have become important targets of current antiretroviral therapies due to the critical role of the limited proteolysis of Gag-Pol polyprotein in the replication cycle and they therefore belong to the most well-studied enzymes. Comparative analyses of retroviral and retroviral-like proteases can help to explore the key similarities and differences which may help understanding how resistance is developed against protease inhibitors, but the available information about the structural and biochemical characteristics of retroviral-like, and especially retrotransposon, proteases is limited. To investigate the main characteristics of Ty1 retrotransposon protease of Saccharomyces cerevisiae, untagged and His6-tagged forms of Ty1 protease were expressed in E. coli. After purification of the recombinant proteins, activity measurements were performed using synthetic oligopeptide and fluorescent recombinant protein substrates, which represented the wild-type and the modified forms of naturally occurring cleavage sites of the protease. We investigated the dependence of enzyme activity on different reaction conditions (pH, temperature, ionic strength, and urea concentration), and determined enzyme kinetic parameters for the studied substrates. Inhibitory potentials of 10 different protease inhibitors were also tested. Ty1 protease was not inhibited by the inhibitors which have been designed against human immunodeficiency virus type 1 protease and are approved as antiretroviral therapeutics. A quaternary structure of homodimeric Ty1 protease was proposed based on homology modeling, and this structure was used to support interpretation of experimental results and to correlate some structural and biochemical characteristics with that of other retroviral proteases.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
retrotransposon
Ty1
protease
retrovirus
homology modeling
ty1 protease
retroviral protease
retrotransposon protease
yeast
biochemical characterization
Megjelenés:Plos One. - 15 : 1 (2020), p. 1-24. -
További szerzők:Matúz Krisztina (1980-) (vegyész, biokémikus) Nagy Tibor (1988-) (vegyész) Mótyán János András (1981-) (biokémikus, molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
GINOP-2.3.3-15-2016-00021
GINOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM086709
035-os BibID:(WoS)000557707400001 (Scopus)85087574382
Első szerző:Golda Mária (molekuláris biológus)
Cím:Biochemical characterization of human retroviral-like aspartic protease 1 (ASPRV1) / Mária Golda, János András Mótyán, Katalin Nagy, Krisztina Matúz, Tibor Nagy, József Tőzsér
Dátum:2020
ISSN:2218-273X
Megjegyzések:The human retroviral-like aspartic protease 1 (ASPRV1) is a mammalian retroviral-like enzyme that catalyzes a critical proteolytic step during epidermal differentiation; therefore, it is also referred as skin-specific aspartic protease (SASPase). Neutrophil granulocytes were also found recently to express ASPRV1 that is involved in the progression of acute chronic in?ammation in the central nervous system, especially in autoimmune encephalomyelitis. Thus, investigation of ASPRV1 is important due to its therapeutic or diagnostic potential. We investigated the structural characteristics of ASPRV1 by homology modeling; analysis of the proposed structure was used for interpretation of in vitro specificity studies. For in vitro characterization, activities of SASP28 and SASP14 enzyme forms were measured using synthetic oligopeptide substrates. We demonstrated that self-processing of SASP28 precursor causes autoactivation of the protease. Highest activity was measured for GST-SASP14 at neutral pH and at high ionic strength, and we proved that pepstatin A and acetyl-pepstatin can also inhibit the protease. In agreement with the structural characteristics, the relatively lower urea dissociation constant implied lower dimer stability of SASP14 compared to that of HIV-1 protease. The obtained structural and biochemical characteristics help better understanding of ASPRV1 function in skin and central nervous system
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
ASPRV1
SASPase
protease
retroviral-like protease
retroviral-like aspartic protease 1
skin-specific aspartic protease
homology modeling
protease inhibitor
Megjelenés:Biomolecules. - 10 : 7 (2020), p. 1-25. -
További szerzők:Mótyán János András (1981-) (biokémikus, molekuláris biológus) Nagy Katalin Matúz Krisztina (1980-) (vegyész, biokémikus) Nagy Tibor (1988-) (vegyész) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
TÁMOP 4.2.2.A-11/1/KONV-2012-0023
TÁMOP
TÁMOP-4.2.2.D-15/1/KONV-2015-0016
TÁMOP
GINOP-2.3.3-15-2016-00021
GINOP
NKFIH-1150-6/2019
Egyéb
K-101591
OTKA
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM089970
035-os BibID:(cikkazonosító)9523 (wos)000602881500001 (scopus)85098234996
Első szerző:Miczi Márió
Cím:Identification of Host Cellular Protein Substrates of SARS-COV-2 Main Protease / Márió Miczi, Mária Golda, Balázs Kunkli, Tibor Nagy, József Tőzsér, János András Mótyán
Dátum:2020
ISSN:1661-6596 1422-0067
Megjegyzések:The novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of coronavirus disease-19 (COVID-19) being associated with severe pneumonia. Like with other viruses, the interaction of SARS-CoV-2 with host cell proteins is necessary for successful replication, and cleavage of cellular targets by the viral protease also may contribute to the pathogenesis, but knowledge about the human proteins that are processed by the main protease (3CLpro) of SARS-CoV-2 is still limited. We tested the prediction potentials of two different in silico methods for the identification of SARS-CoV-2 3CLpro cleavage sites in human proteins. Short stretches of homologous host-pathogen protein sequences (SSHHPS) that are present in SARS-CoV-2 polyprotein and human proteins were identified using BLAST analysis, and the NetCorona 1.0 webserver was used to successfully predict cleavage sites, although this method was primarily developed for SARS-CoV. Human C-terminal-binding protein 1 (CTBP1) was found to be cleaved in vitro by SARS-CoV-2 3CLpro, the existence of the cleavage site was proved experimentally by using a His6-MBP-mEYFP recombinant substrate containing the predicted target sequence. Our results highlight both potentials and limitations of the tested algorithms. The identification of candidate host substrates of 3CLpro may help better develop an understanding of the molecular mechanisms behind the replication and pathogenesis of SARS-CoV-2.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
host protein cleavage
cleavage site prediction
cleavage site identification
SSHHPS
NetCorona
COVID-19
SARS
SARS-CoV-2
protease
3CL protease
coronavirus
main protease
Megjelenés:International Journal Of Molecular Sciences. - 21 : 24 (2020), p. 1-19. -
További szerzők:Golda Mária (1986-) (molekuláris biológus) Kunkli Balázs Nagy Tibor (1988-) (vegyész) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Mótyán János András (1981-) (biokémikus, molekuláris biológus)
Pályázati támogatás:GINOP-2.3.3-15-2016-00021
GINOP
NKFIH-1150-6/2019
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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5.

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
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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