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001-es BibID:	BIBFORM001058
Első szerző:	Zajácz Ágnes
Cím:	Aleppo tannin : structural analysis and salivary amylase inhibition / Ágnes Zajácz, Gyöngyi Gyémánt, Natale Vittori, Lili Kandra
Dátum:	2007
Megjegyzések:	The effectiveness and specificity of a tannin inhibition on human salivary amylase (HSA) catalysed hydrolysis was studied using 2-chloro-4-nitrophenyl 4-O-?-D-galactopyranosyl-?-D-maltoside (GalG2-CNP) and amylose substrates. Aleppo tannin was isolated from the gall nut of Aleppo oak. This tannin is a gallotannin, in which glucose is esterified with gallic acids. This is the first kinetic report, which details the inhibitory effects of this compound on HSA. A mixed non-competitive type inhibition has been observed on both substrates. The extent of inhibition is markedly dependent on the substrate-type. Kinetic constants were calculated from Lineweaver-Burk secondary plots for GalG2-CNP (KEI 0.82 ?g mL-1, KESI 3.3 ?g mL-1). This indicates a 1:1 binding ratio of inhibitor-enzyme and/or inhibitor-enzyme-substrate complex. When amylose was the substrate the binding ratio of inhibitor to enzyme-substrate complex was found to be 2:1, with the binding constants of KEI 17.4 ?g mL-1, KESI 14.9 ?g mL-1, KESI2 9.6 ?g mL-1. Presumably, the tannin inhibitor can bind not only to HSA, but to the amylose substrate, as well. Kinetic data suggest that aleppo tannin is a more efficient amylase inhibitor than the recently studied other tannin with quinic acid core (GalG2-CNP: KEI 9.0 ?g mL-1, KESI 47.9 ?g mL-1).
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban amiláz inhibíció gallotannin szerkezet-analízis
Megjelenés:	Carbohydrate Research. - 342 : 5 (2007), p. 717-723. -
További szerzők:	Vittori, Natale Gyémánt Gyöngyi (1960-) (vegyész) Kandra Lili (1943-) (biokémikus)
Pályázati támogatás:	T047075 OTKA
Internet cím:	Elektronikus változat DOI Szerző által megadott URL
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