Diets fed to nonruminant animals are composed mainly of feed ingredients of plant origin. A variety of antinutritional factors such as phytin, nonstarch polysaccharides, and protease inhibitors may be present in these feed ingredients, which could limit nutrients that may be utilized by animals fed such diets. The primary nutrient utilization-limiting effect of phytin arises from the binding of 6 phosphate groups, thus making the P unavailable to the animal. The negative charges allow for formation of insoluble phytin-metal complexes with many divalent cations. Furthermore, phytin and protein can form binary complexes through electrostatic links of its charged phosphate groups with either the free amino group on AA on proteins or via formation of ternary complexes of phytin, Ca(2+), and protein. The form and extent of de novo formation of binary and ternary complexes of phytin and protein are likely to be important variables that influence the effectiveness of nutrient hydrolysis in plant-based diets. Nonstarch polysacharides reduce effective energy and nutrient utilization by nonruminant animals because of a lack of the enzymes needed for breaking down the complex cell wall structure that encapsulate other nutrients. Enzymes are used in nonruminant animal production to promote growth and efficiency of nutrient utilization and reduce nutrient excretion. The enzymes used include those that target phytin and nonstarch polysaccharides. Phytase improves growth and enhances P utilization, but positive effects on other nutrients are not always observed. Nonstarch polysaccharide-hydrolyzing enzymes are less consistent in their effects on growth and nutrient utilization, although they show promise and it is imperative to closely match both types and amounts of nonstarch polysaccharides with appropriate enzyme for beneficial effects. When used together with phytase, nonstarch polysaccharide-hydrolyzing enzymes may increase the accessibility of phytase to phytin encapsulated in cell walls. The future of enzymes in nonruminant animal production is promising and will likely include an understanding of the role of enzyme supplementation in promoting health as well as how enzymes may modulate gene functions. This review is an attempt to summarize current thinking in this area, provide some clarity in nomenclature and mechanisms, and suggest opportunities for expanded exploitation of this unique biotechnology.

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Protein–phytate interactions are fundamental to the detrimental impact of phytate on protein/amino acid availability. The inclusion of exogenous phytase in pig and poultry diets degrades phytate to more innocuous esters and attenuates these negative influences. The objective of the present review is to reappraise the underlying mechanisms of these interactions and reassess their implications in pig and poultry nutrition. Protein digestion appears to be impeded by phytate in the following manner. Binary protein–phytate complexes are formed at pH levels less than the isoelectric point of proteins and complexed proteins are refractory to pepsin digestion. Once the protein isoelectric points are exceeded binary complexes dissociate; however, the isoelectric point of proteins in cereal grains may be sufficiently high to permit these complexes to persist in the small intestine. Ternary protein–phytate complexes are formed at pH levels above the isoelectric point of proteins where a cationic bridge links the protein and phytate moieties. The molecular weights of protein and polypeptides in small-intestinal digesta may be sufficient to allow phytate to bind nutritionally important amounts of protein in ternary complexes. Thus binary and ternary complexes may impede protein digestion and amino acid absorption in the small intestine. Alternatively, phytate may interact with protein indirectly.Myo-inositol hexaphosphate possesses six phosphate anionic moieties (HPO42–) that have strong kosmotropic effects and can stabilise proteins by interacting with the surrounding water medium. Phytate increases mucin secretions into the gut, which increases endogenous amino acid flows as the protein component of mucin remains largely undigested. Phytate promotes the transition of Na+into the small-intestinal lumen and this suggests that phytate may interfere with glucose and amino acid absorption by compromising Na+-dependent transport systems and the activity of the Na pump (Na+-K+-ATPase). Starch digestion may be depressed by phytate interacting with proteins that are closely associated with starch in the endosperm of cereal grains. While elucidation is required, the impacts of dietary phytate and exogenous phytase on the site, rate and synchrony of glucose and amino acid intestinal uptakes may be of importance to efficient protein deposition. Somewhat paradoxically, the responses to phytase in the majority of amino acid digestibility assays in pigs and poultry are equivocal. A brief consideration of the probable reasons for these inconclusive outcomes is included in this reappraisal.