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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
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM018946
Első szerző:	Mótyán János András (biokémikus, molekuláris biológus)
Cím:	Transglycosylation by barley alfa-amylase 1 / Mótyán János A., Fazekas Erika, Mori Haruhide, Svensson Birte, Bagossi Péter, Kandra Lili, Gyémánt Gyöngyi
Dátum:	2011
ISSN:	1381-1177
Megjegyzések:	The transglycosylation activity of barley alfa-amylase 1 (AMY1) and active site AMY1 subsite mutant enzymes was investigated. We report here the transferase ability of the V47A, V47F, V47D and S48Y single mutants and V47K/S48G and V47G/S48D double mutant AMY1 enzymes in which the replaced amino acids play important role in substrate binding at subsites at-3 through-5. Although mutation increases the transglycosylation activity of enzymes, in the presence of acceptors the difference between wild type and mutants is not so significant. Oligomer transfer reactions of AMY1 wild type and its mutants were studied using maltoheptaose and maltopentaose donors and different chromophore containing acceptors. The conditions for the chemoenzymatic synthesis of 4-methylumbelliferyl-alfa-d-maltooligosaccharides (MU-alfa-d-MOSs) were optimized using 4-methylumbelliferyl-alfa-d-glucoside as acceptor and maltoheptaose as donor. 4-Methylumbelliferyl-alfa-d-maltoside, -maltotrioside, -maltotetraoside and -maltopentaoside have been synthesized. Products were identified by MALDI-TOF MS. 1H and 13C NMR analyses showed that AMY1 V47F preserved the stereo- and regioselectivity. The produced MU-alfa-d-MOSs of degree of polymerization DP 2, DP 3 and DP 5 were successfully applied to detect activity of Bacillus stearothermophilus maltogenic alfa-amylase, human saliv
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Barley alpha-amylase 1 Transglycosylation Methylumbelliferyl-glycosides Chemoenzymatic synthesis Amylase assay
Megjelenés:	Journal Of Molecular Catalysis B-Enzymatic. - 72 : 3-4 (2011), p. 229-237. -
További szerzők:	Fazekas Erika (1985-) (kémikus) Mori, Haruhide Svensson, Birte Bagossi Péter (1966-2011) (biokémikus, vegyész) Kandra Lili (1943-) (biokémikus) Gyémánt Gyöngyi (1960-) (vegyész)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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