Structure elucidation of catechins for modulation of starch digestion.

Miao, M., Jiang, H., Jiang, B., Li, Y., Cui, S.W., and Zhang, T. (2014). "Structure elucidation of catechins for modulation of starch digestion.", Food Science and Technology - LWT, 57(1), pp. 188-193. doi : 10.1016/j.lwt.2014.01.005  Access to full text

Abstract

This study investigated interactions of six type catechins monomers with human pancreatic α-amylase and the structural requirements for inhibitory activity. The in vitro and in silico results showed that inhibitory effects of catechins followed the order: (+)-gallocatechin-3-O-gallate > (−)-epicatechin-3-O-gallate > (−)-epigallocatechin-3-O-gallate > (−)-epicatechin > (−)-epigallocatechin > (+)-catechin. The A, B and C rings of catechins affected the activity by interact with the catalytic residues of the active site of α-amylase forming a phenols–protein complex, including hydroxyl on the 3-position or 5-position of A–C rings, number of hydroxyl substation on the B-ring or C ring, or 2,3-cis/trans isomerism. The galloylated catechins has higher binding affinity with α-amylase than non-galloylated catechins. The results showed that biological activity of catechins against α-amylase, which supported catechins monomer is a promising ingredient as a development strategy of health food for regulation of energy balance and reduction of related diseases risk.

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