Hydrolysable Tannin–Protein Interactions: The Devil Is in the Structural Details

 

Tannins and their various bioactivities have been studied for decades because of the multiple bioactivities they express. Due to the high number of studies carried out with various methods, varying tannin and protein sources as well as variable tannin purities, it is difficult to combine these results and fashion them into a meaningful whole. Moreover, regarding bioactivity, the devil is in the details and small changes in tannin structure may drastically alter the obtained bioactivity.

Our ultimate goal is to be able to predict the bioactivities of not yet studied compounds directly from their structural features. In the present work, we chose altogether 32 tannins from multiple branches of the biosynthetic pathway of hydrolysable tannins to make conclusions on their protein precipitation capacity and the compositions of the formed complexes. For this, we utilised a turbidimetric plate reader method and ultrahigh performance liquid chromatography with diode array detection.

Our results indicated clear relationships between the structural features of hydrolysable tannins and their ability to form insoluble complexes with the model protein. In addition, the compositions of the formed complexes depended on the exact tannin structure. Altogether, our results highlighted the importance of the structural details of tannins to better understand their various bioactivities and possible use in different applications.

Authors declare no conflicts of interest.

Publication History

Article published online:
12 December 2022

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