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Feed enzymes
| Catalog | Product Name | EC No. | CAS No. | Source | Price |
|---|---|---|---|---|---|
| AGT-2913 | Feed enzyme designed by wheat and its by-products | Inquiry |
Related Reading
Introductions
The use of exogenous feed enzymes in poultry diets is becoming a norm to overcome the adverse effects of antinutritional factors and improve digestion of dietary components and bird performance.
Characteristics of Enzymes
To better understand the limits of feed enzyme usage, the fundamental characteristics of enzymes need to be considered first. Enzymes are highly effective biological catalysts capable of accelerating chemical reactions millions of times over, in some cases. Chemically, they are proteins with a highly complex three-dimensional molecular structure. The protein nature of enzymes has important implications for their stability during high-temperature feed manufacture and transit through the gastrointestinal tract. As proteins, they can be denatured by heat and pH and they can also be subject to proteolysis by digestive enzymes.
Classifications
Four different classes of feed enzyme products are currently available on the market for use in the feed industry: (1) microbial phytase, (2) polyglycosidases for cohesive grains (e.g., wheat, barley), (3) enzymes for non-cohesive grains (e.g., corn, sorghum), and (4) enzymes for non-cohesive grains (e.g., soybean meal, beans). With the exception of microbial phytase, most other enzyme products contain a mixture of enzymes that may be produced by one or more organisms. There is evidence that preparations with multiple enzyme activities may provide a competitive strategy to improve nutrient utilization in poultry diets.
Table 1. Type of commercial feed enzymes and target substrates
| Enzyme | Target substrate | Target feedstuff |
| Phytases | Phytic acid | All plant-derived ingredients |
| B-Glucanase | 3-Glucan | Barley, oats, and rye |
| Xylanases | Arabinoxylans | Wheat, rye, triticale, barley, fibrous plant materials |
| a-Galactosidases | Oligosaccharides | Soybean meal, grain legumes |
| Proteases | Proteins | All plant protein sources |
| Amylase | Starch | Cereal grains, grain legumes |
| Lipases | Lipids | Lipids in feed ingredients |
| Mannanases, cellulases, hemicellulasespectinases | Cell wall matrix (fibercomponents) | Plant-derived ingredients, fibrous plant materials |
Carbohydrases
Carbohydrase is the name of a set of enzymes that catalyze 5 types of reactions, turning carbohydrates into simple sugars, from the large family of glycosidases. Carbohydrases are produced in the pancreas, salivary glands and small intestine, breaking down polysaccharides. This is because complex sugars are often insoluble (such as starch), and therefore breaking them down will make it easier for the sugars to be absorbed into the blood, through the wall of the small intestine. A carbohydrate is usually a compound consisting of carbon, hydrogen and oxygen. Carbohydrase facilitates the hydrolysis of polysaccharides into simpler sugars called Monosaccharides.
Phytase
A phytase (myo-inositol hexakisphosphate phosphohydrolase) is any type of phosphatase enzyme that catalyzes the hydrolysis of phytic acid (myo-inositol hexakisphosphate) – an indigestible, organic form of phosphorus that is found in many plant tissues, especially in grains and oil seeds – and releases a usable form of inorganic phosphorus. While phytases have been found to occur in animals, plants, fungi and bacteria, phytases have been most commonly detected and characterized from fungi.
Proteases
Proteases likely arose at the earliest stages of protein evolution as simple destructive enzymes necessary for protein catabolism and the generation of amino acids in primitive organisms. For many years, studies on proteases focused on their original roles as blunt aggressors associated with protein demolition. However, the realization that, beyond these nonspecific degradative functions, proteases act as sharp scissors and catalyze highly specific reactions of proteolytic processing, producing new protein products, inaugurated a new era in protease research.