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Creative Enzymes' services are beyond the average level in the enzyme industries. Powered by the cutting-edge instruments and skillful operations, our services feature reliable test results with a quick turn-around time. Our knowledgeable scientists are of extensive experiences and can perform suitable assays to determine the activity of 4-phytase.
Phytase is a member of the histidine acid phosphatase family which share a consensus sequence pattern. Phytase is able to catalyze the hydrolysis of phosphomonoester bonds of phytate, releasing lower forms of myo-inositol phosphates and inorganic phosphate. Depended on the position of the first phosphate in the inositol ring to be removed, phytases are divided into three classes, one of which is 4-phytase (EC 3.1.3.26).
Phytate is a widely distributed natural substance found in plants. It is the primary source of inositol and the primary storage form of phosphate in seeds. Seeds are not only important components of food for humans but also vital ingredients for animal feed preparations. However, monogastric animals, like poultry and pig, are unable to utilize the phosphorus in phytate because the phytase activity is too low to achieve efficient digestion. Furthermore, phytate acts as an anti-nutrient substance due to its ability to chelate divalent cations, thus preventing the uptake of minerals. Therefore, phytases, which hydrolize phytates, are used as a cereal feed additive that enhances the phosphorus and mineral uptake. In addition, excretion of phytate in the livestock production can lead to the accumulation of phosphate in soil and water, and subsequently to eutrophication of fresh water streams and near coastal seawaters. In this regard, phytase has potentials in environmental pollution control. Considering the applications in agriculture and biotechnology, more and more studies are targeted for phytases, including 4-phytase. Creative Enzymes provides precise activity assay services for 4-phytase to support the needs in fundamental research.
Figure: The crystal structure of phytase from Hafnia Alvei in complex with tartrate.
Reference: Ariza, A. et al. PLoS One. 2013 8(5): e65062.
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