Abstract
The complexation of several tannic acids (purified tannins) with soluble and insoluble proteins has been studied by high-performance liquid chromatography, Tannins are analysed in both the straight phase and the reversed-phase mode. Bovine serum albumin (BSA) and beer proteins were chromatographed in the size exclusion mode. Soluble proteins seem to complex preferentially with the higher molecular weight tannin polygalloyl glucose components, whereas insoluble standardized hide powder binds preferentially to lower molecular weight tannin components. The tanning capacity of different tannic acids can be expressed in milligrams of BSA bonded per milligram of tannin under standard conditions.
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