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

被引:124
作者
Sun, Lijun [1 ]
Warren, Fredrick J. [1 ,2 ]
Netzel, Gabriele [1 ]
Gidley, Michael J. [1 ]
机构
[1] Univ Queensland, Ctr Nutr & Food Sci, ARC Ctr Excellence Plant Cell Walls Queensland Al, Brisbane, Qld 4072, Australia
[2] Inst Food Res, Norwich Res Pk, Norwich NR4 7UA, Norfolk, England
基金
英国生物技术与生命科学研究理事会; 澳大利亚研究理事会;
关键词
Tea polyphenols; alpha-Amylase; Inhibition; Kinetics; Galloyl moiety; DIRECT LINEAR PLOT; GREEN TEA; STARCH DIGESTION; BLACK TEA; GLUCOSIDASE ACTIVITY; IN-VITRO; MECHANISM; EXTRACT; TANNINS; BINDING;
D O I
10.1016/j.jff.2016.07.012
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The inhibitory activities of three tea extracts (TEs) and individual phenolic compounds in TEs against porcine pancreatic alpha-amylase (PPA) were studied by measuring their half inhibitory (IC50) concentrations. The kinetics of inhibition by these extracts and compounds were investigated through Dixon, Cornish-Bowden, and Lineweaver-Burk plots. The results showed that green, oolong and black tea extracts, epigallocatechin gallate, theaflavin-3, 3'-digallate and tannic acid were competitive inhibitors of PPA, whereas epicatechin gallate, theaflavin-3'-gallate and theaflavin were mixed-type inhibitors with both competitive and uncompetitive inhibitory characteristics. Only catechins with a galloyl substituent at the 3-position showed measurable inhibition. The competitive inhibition constants (Ku) were lower for theaflavins than catechins, with the lowest value for theaflavin-3, 3'-digallate. The lower than the uncompetitive inhibition constant for the mixed-type inhibitors suggests that they bind more tightly with free PPA than with the PPA-starch complex. A 3 and/or 3'-galloyl moiety in catechin and theaflavin structures was consistently found to increase inhibition of PPA through enhanced association with the enzyme active site. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码:144 / 156
页数:13
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