Representative condensed and hydrolyzable tannins and related simple phenolics were evaluated as biological antioxidants using cyclic voltammetry, the metmyoglobin assay, and the deoxyribose assay. The redox potentials of the tannins were similar to those of structurally related simple phenolics. However, the tannins were 15-30 times more effective at quenching peroxyl radicals than simple phenolics or Trolox. One of the tannins, polygalloyl glucose, reacted an order of magnitude more quickly with hydroxyl radical than mannitol. These results suggest that tannins, which are found in many plant-based foods and beverages, are potentially very important biological antioxidants.

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We tested the hypothesis that tannins defend plants against large herbivores by decreasing protein availability. Digestion trials were conducted with mule deer (Odocoileus hemionus) and results from previous trials with white—tailed deer (O. virginianus), moose (Alces alces), caribou/reindeer (Rangifer tarandus), and elk (Cervus elaphus) were summarized to evaluate dietary factors affecting protein availability. The digestibility of plant protein in feeds with minimal tannins, such as grasses and agriculturally produced legumes and grains, was a highly predictable function of the total protein content and the amount of nondigestible, fiber—bound protein. Digestible protein in plants containing significant tannins was lower than predicted from regressions for low—tannin feeds. The reduction in digestible protein was proportional to the protein—precipitating capacity of the plant tannins. Deciduous browse stems collected in winter had very low levels of protein—precipitating tannins and only a slightly lower protein availability than predicted. Tannins are not important in the defense of most deciduous tree shrub stems consumed by these herbivores. Tannins in flowers and forb, tree, and shrub leaves markedly reduced protein availability. Tannins must be considered in understanding the defensive strategies of leaves and flowers. Voluntary intake of the high—phenolic forages was significantly reduced below ingestion rates for grasses, legumes, and pelleted diets. It is hypothesized that soluble phenolics that do not inhibit digestion but are absorbed and reduced intake through their toxicity are more important in defending some plant parts against ruminants than are digestion—reducing tannins.

Tannin in plant extracts can be determined by reacting the tannin with a protein and quantitating the precipitated complex. In the new assay described here, a tannin-containing solution is placed in a well in a protein-containing agar slab. As the tannin diffuses into the gel and complexes with protein, a visible ring of precipitation develops. The area of the ring is proportional to the amount of tannin in the extract. The detection limit of the method is 0.025 mg tannic acid or condensed tannin and the precision is 6% (relative standard deviation). Tests with extracts of a variety of plants show that the new method gives results comparable to other precipitation methods and that the new method is superior for samples of unusual composition, such as aspen buds. The method has several advantages over other methods for determining tannin: The new method is very simple and requires neither complex reagents nor instruments. Components of the plant extract such as non-tannin phenolics or water-insoluble compounds do not interfere with the method. The assay is not subject to interference from the organic and aqueous solutions which are commonly used to extract tannin from plants.

The precipitates that form when purified pentagalloylglucose or a purified procyanidin [epicatechin16 (4→8) catechin; EC16-C] are mixed with bovine serum albumin were quantitatively analyzed. EC16-C is a more efficient protein precipitating agent than pentagalloylglucose on a molar or a mass basis. EC16-C precipitates protein independently of temperature and presence of organic solvent. Precipitation by pentagalloylglucose increases as temperature is increased and decreases when alcohols are present. When tannin is in excess, up to 40 mol of pentagalloylglucose is bound per mole of protein precipitated, but only 20 mol of EC16-C is bound per mole of protein precipitated. The data support different models of precipitation for the two types of tannin:  pentagalloylglucose, which is very nonpolar, precipitates by forming a hydrophobic coat around the protein, whereas the much more polar EC16-C forms hydrogen-bonded cross-links between protein molecules. Keywords: Polyphenol−protein interaction; tannin; pentagalloylglucose; procyanidin; condensed tannin; bovine serum albumin