3 or 3’-Galloyl substitution plays an important role in association of catechins and theaflavins with porcine pancreatic α-amylase: The kinetics of inhibition of α-amylase by tea polyphenols
作者： Lijun Sun , Fredrick J. Warren , Gabriele Netzel , Michael J. Gidley
DOI: 10.1016/J.JFF.2016.07.012
关键词:
摘要: Abstract The inhibitory activities of three tea extracts (TEs) and individual phenolic compounds in TEs against porcine pancreatic α-amylase (PPA) were studied by measuring their half (IC50) concentrations. kinetics inhibition these investigated through Dixon, Cornish-Bowden, Lineweaver–Burk plots. results showed that green, oolong black extracts, epigallocatechin gallate, theaflavin-3, 3′-digallate tannic acid competitive inhibitors PPA, whereas epicatechin theaflavin-3′-gallate theaflavin mixed-type with both uncompetitive characteristics. Only catechins a galloyl substituent at the 3-position measurable inhibition. constants (Kic) lower for theaflavins than catechins, lowest value 3′-digallate. Kic constant suggests they bind more tightly free PPA PPA–starch complex. A 3 and/or 3′-galloyl moiety catechin structures was consistently found to increase enhanced association enzyme active site.
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