Formation of complexes between tannic acid with bovine serum albumin, egg ovalbumin and bovine beta-lactoglobulin

Tannic acid (TA) shows strong interactions with proteins and the resulting complexes can be utilized as delivery systems for oral drugs. The complexation of TA with three proteins including bovine serum albumin (BSA), egg ovalbumin (EA) and bovine beta-lactoglobulin (BLG) at pH 7.4 was studied. The tryptophan (Trp) fluorescence of all three proteins was quenched by TA in a static quenching mechanism. BLG showed the highest binding affinity and a...