Aleppo tannin: structural analysis and salivary amylase inhibition

Ágnes Zajácz, Gyöngyi Gyémánt, Natale Vittori, Lili Kandra

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28 Citations (Scopus)


The effectiveness and specificity of a tannin inhibition on human salivary amylase (HSA) catalyzed hydrolysis was studied using 2-chloro-4-nitrophenyl 4-O-β-d-galactopyranosyl-α-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 μg mL-1, KESI 3.3 μg 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 μg mL-1, KESI 14.9 μg mL-1, KESI2 9.6 μg 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 μg mL-1, KESI 47.9 μg mL-1).

Original languageEnglish
Pages (from-to)717-723
Number of pages7
JournalCarbohydrate Research
Issue number5
Publication statusPublished - Apr 9 2007


  • Aleppo tannin
  • Gallotannin
  • HSA
  • Inhibitor
  • Kinetic analysis

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry

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