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001-es BibID:	BIBFORM079356
Első szerző:	Kandra Lili (biokémikus)
Cím:	Chemoenzymatic synthesis of 2-chloro-4-nitrophenyl β-maltoheptaoside acceptor-products using glycogen phosphorylase b / Kandra Lili, Gyémánt Gyöngyi, Pál Magda, Petró Marianna, Remenyik Judit, Lipták András
Dátum:	2001
ISSN:	0008-6215
Megjegyzések:	In the present work, we aimed at developing a chemoenzymatic procedure for the synthesis of β-maltooligosaccharide glycosides. The primer in the enzymatic reaction was 2-chloro-4-nitrophenyl β-maltoheptaoside (G7-CNP), synthesised from β-cyclodextrin using a convenient chemical method. CNP-maltooligosaccharides of longer chain length, in the range of DP 8-11, were obtained by a transglycosylation reaction using α-d-glucopyranosyl-phosphate (G-1-P) as a donor. Detailed enzymological studies revealed that the conversion of G7-CNP catalysed by rabbit skeletal muscle glycogen phosphorylase b (EC 2.4.1.1) could be controlled by acarbose and was highly dependent on the conditions of transglycosylation. More than 90% conversion of G7-CNP was achieved through a 10:1 donor-acceptor ratio. Tranglycosylation at 37 °C for 30 min with 10 U enzyme resulted in G8?12-CNP oligomers in the ratio of 22.8, 26.6, 23.2, 16.5, and 6.8%, respectively. The reaction pattern was investigated using an HPLC system. The preparative scale isolation of G8?11-CNP glycosides was achieved on a semipreparative HPLC column. The productivity of the synthesis was improved by yields up to 70-75%. The structures of the oligomers were confirmed by their chromatographic behaviours and MALDI-TOF MS data.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Maltooligosaccharide series Transglycosylation Glycogen phosphorylase b Chain elongation
Megjelenés:	Carbohydrate Research. - 333 : 2 (2001), p. 129-136. -
További szerzők:	Gyémánt Gyöngyi (1960-) (vegyész) Pál Magda Petró Marianna Gálné Remenyik Judit (1965-) (kémia tanár, okleveles vegyész) Lipták András (1935-2012) (vegyész)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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