Reevaluation of Phytase Action Mechanism in Animal Nutrition

Abstract

The release of phosphorus from phytates occurs via sequential cleavage of phosphate groups. It was believed that, regardless of the properties of phytases, the rate of phytate dephosphorylation is limited by the first cleavage of any phosphate group. The position of the first cleaved-off phosphate group depending on the specificity of phytase. The inhibition of dephosphorylation initiation is not associated with the action mechanism of the enzyme and can be rather due to the insufficient phytase activity or low availability of phytates. The analysis of the transformations in the inositol hexakisphosphate (IP6)→inositol (I) reaction chain shows that IP6 dephosphorylation as a whole limits the phosphate group removal from I(1,2,5,6)P4 (third reaction from the beginning of hydrolysis of phosphate bonds in PA). The lower availability of nutrients in the presence of phytates is not due to action of phytates, but is caused by PA anions (IP6-3), which bind positively charged metal ions, amino acids, and proteins. The availability of nutrients increases as a result of the decrease in their binding caused by the decrease in the concentration of IP(6-3) anions under the action of phytases. Phytases added to feeds play a lesser role in the digestion of phytates compared to natural enzymes and complement their action. The concept of extra-phosphoric effect has no scientific justification, since phytases exhibit only the phosphohydrolase activity and are not able to catalyze other reactions.