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文献信息

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

期刊名:Journal of Functional Foods
文献编号:
文献地址: http://www.sciencedirect.com/science/article/pii/S1756464616301918
发表日期:October 2016
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 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 (Kic) were lower for theaflavins than catechins, with the lowest value for theaflavin-3, 3′-digallate. The lower Kic 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.

... gallate (
EGCG, C 22 H 18 O 11 ), (-)epicatechin gallate (ECG, C 22 H 18 O 10 ), theaflavin (TF, C 29 H 24 O 12 ), theaflavin-3′-gallate (TF1, C 36 H 28 O 16 ), and theaflavin-3, 3′-digallate (TF2, C 43 H 32 O 20 ) were obtained from Chengdu Biopurify Phytochemicals Ltd. ...