Structural Features of Hydrolyzable Tannins Determine Their Ability to Form Insoluble Complexes with Bovine Serum Albumin.

Abstract

The ability of 32 purified and characterized hydrolyzable tannins to form insoluble complexes with model protein bovine serum albumin was investigated with a turbidimetric 96-well plate reader method. The results showed a clear relationship between the hydrolyzable tannin structure and the intensity of haze that formed during the tannin-protein complexation. In addition to molecular weight, structural features such as number of galloyl groups, degree of oxidative coupling between the galloyls, positional isomerism, and cyclic vs acyclic glucose core were the major structural features that affected the ability of the monomeric hydrolyzable tannins to form insoluble complexes with bovine serum albumin. While oligomers were superior to monomers in their capability to precipitate the model protein, their activity depended less on the functional groups, but mostly on their size and overall flexibility. These results allowed us to construct an equation that predicted the protein precipitation capacity of the studied hydrolyzable tannins with high accuracy.