Dixon, Cornish-Bowden and Lineweaver-Burk plot analyses were applied to study the detailed kinetics of inhibition of porcine pancreatic α-amylase (PPA) by tea polyphenols.Fluorescence quenching (FQ), differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC) were combined with the kinetics of inhibition to elucidate the mechanism of binding interactions of tea polyphenols and PPA. Then, the reciprocal of competitive inhibition constant (1/K ic ), fluorescence quenching constant (K FQ ) and binding constant (K itc ) obtained from these measurements were compared and correlated to analyse the relations between PPA inhibition and binding behaviour. The role of the galloyl moiety in binding of catechins and theaflavins with PPA was highlighted as well. In addition, the effects of three soluble polysaccharides (citrus pectin (CP), wheat arabinoxylan (WAX) and oat β-glucan (OBG)) on the inhibition of PPA by tea polyphenols were studied through PPA inhibition, IC 50 value, inhibition kinetics and fluorescence quenching methods. Furthermore, the effects of tea polyphenols on binding of PPA with normal maize starch granules were studied in terms of binding ratio, dissociation constant (K d ) and binding rate. Then, the association constant (1/K d ), 1/K ic and K FQ of tea polyphenols were correlated to analyse the effects of PPA inhibition on the binding of the enzyme with starch.The results show 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. K ic values were lower for theaflavins than catechins, with the lowest value for theaflavin-3, 3'-digallate. The lower K ic 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. A higher quenching effect of polyphenols corresponded to a stronger inhibitory activity against PPA. The red-shift of maximum emission wavelength of PPA bound with some polyphenols indicated a potential IV