Abstract
Effects of acidic and alkaline treatments on tannic acid (TA), one of the hydrolyzable tannins, and its binding property to protein [bovine serum albumin (BSA)] were investigated. Dissociation of TA-BSA complexes was apparent in both highly acidic and alkaline treatments. TA dissociate from the complexes and pure TA was not hydrolyzed in highly acidic media and retained its protein-binding property. TA did not seem to be hydrolyzed even with a more acidic treatment, although its protein-binding property was much reduced. The higher pH treatment faciliated the hydrolysis of TA, as judged by the release of its constituent gallic acid
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