CCL

Összesen 3 találat.
#/oldal:
Részletezés:
Rendezés:

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
Borító:

2.

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
Borító:

3.

001-es BibID:BIBFORM104263
035-os BibID:(cikkazonosító)999233 (Scopus)85141175162 (WOS)000888173300001 (PubMed)36341352
Első szerző:Miltner Noémi (molekuláris biológus)
Cím:Early suppression of antiviral host response and protocadherins by SARS-CoV-2 Spike protein in THP-1-derived macrophage-like cells / Miltner Noémi, Linkner Tamás Richárd, Ambrus Viktor, Al-Muffti Aya S., Ahmad Hala, Mótyán János András, Benkő Szilvia, Tőzsér József, Mahdi Mohamed
Dátum:2022
ISSN:1664-3224
Megjegyzések:The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of coronavirus disease-19 (COVID-19). The spike protein (S) of SARS-CoV-2 plays a crucial role in mediating viral infectivity; hence, in an extensive effort to curb the pandemic, many urgently approved vaccines rely on the expression of the S protein, aiming to induce a humoral and cellular response to protect against the infection. Given the very limited information about the effects of intracellular expression of the S protein in host cells, we aimed to characterize the early cellular transcriptomic changes induced by expression of the S protein in THP-1-derived macrophage-like cells. Results showed that a wide variety of genes were differentially expressed, products of which are mainly involved in cell adhesion, homeostasis, and most notably, antiviral and immune responses, depicted by significant downregulation of protocadherins and type I alpha interferons (IFNAs). While initially, the levels of IFNAs were higher in the medium of S protein expressing cells, the downregulation observed on the transcriptomic level might have been reflected by no further increase of IFNA cytokines beyond the 5 h time-point, compared to the mock control. Our study highlights the intrinsic pathogenic role of the S protein and sheds some light on the potential drawbacks of its utilization in the context of vaccination strategies.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
SARS-CoV-2
coronavirus
COVID-19
spike protein
transcriptomics
virology
Megjelenés:Frontiers in Immunology. - 13 (2022), p. 999233. -
További szerzők:Linkner Tamás Richárd Ambrus Viktor Attila (1989-) (biotechnológus) Al-Muffti, Aya S. Ahmad, Hala Mótyán János András (1981-) (biokémikus, molekuláris biológus) Benkő Szilvia (1973-) (molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Mahdi, Mohamed (1979-) (orvos, tudományos segédmunkatárs)
Pályázati támogatás:TKP2021-EGA-20
Egyéb
POST-COVID2021-16
Egyéb
K131844
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Rekordok letöltése1