Phytochemicals and digestion

Feedstuffs consist largely of complex polymers (e.g. proteins, starches, fats) that must be hydrolyzed to the constituent building blocks before they can be absorbed and made available to the host. The digestibility of many plant proteins is inherently lower compared to proteins from animal tissues. This is particularly true for the structural proteins (Carbonaro et al, 2000 Mariotti et al, 1999). As a consequence, amino acid scores for many plant proteins often do not reflect true availability to the host (Mariotti et al, 2001). 

Second, the presence of anti-nutrients requires heightened stimulation of digestive secretions (Santoro et ah, 1997). This increases the costs of digestion, which are already appreciable (Tamminga et al, 1995). 

The complex polymers in feedstuffs are broken down to the constituent building blocks by a sequential process. Hydrolysis of the polymers is initiated in the lumen of the GIT by enzymes and other secretions produced by the pancreas, stomach, intestine, liver and gall bladder, and other GIT tissues, and completed by another suite of enzymes associated with the brush border membrane (BBM) or intracellular organelles. Anti-nutrient phytochemicals can decrease the hydrolysis of feedstuffs, and thereby reduce nutrient availability, either by increasing the inherent resistance of the polymers to hydrolysis or by decreasing the activities or amounts of enzymes and other secretions produced by the GIT. 

Some of the best investigated anti-nutrients are the enzyme inhibitors present in legumes and other plants. The Bowman-Birk and the Kunitz inhibitors of trypsin and other proteases are among the best characterized. In contrast to the non-specific and widespread influences of tannins and lectins (Carmona, 1996), the Bowman-Birk, Kunitz and other such inhibitors target specific enzymes. Corresponding with this, proteases and other digestive enzymes vary in sensitivity to the different inhibitors. 

In addition to proteases, other inhibitors reduce the activity of amylase and other digestive enzymes (Ishimoto et al, 1999). Many varieties of beans produce a glycoprotein that complexes with and inhibits a-amylase (Mirkov et al, 1995). The amylase inhibitors are non-competitive and thermostable (Gallaher and Schneeman, 1986) and, unlike protease inhibitors, do not elicit heightened secretion of amylase (Toskes, 1986). Although over-expression 

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