Preparations of phytate-degrading enzymes have a variety of uses in animal and human nutrition. These enzymes also attract a lot of attention from entrepreneurs and scientists in the fields of biotechnology and environmental protection.
Biotechnological applications of phytotases, especially for the reduction in phytate in feed and food, are very interesting. The best high quality of phytase enzymes can initiate the stepwise release of myoinositol, phosphoric acid, and the formation of myoinositol phosphate intermediates from phytotate.
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Most plant-origin foods contain between 50% and 80% of total phosphorus as phytotate. Phytate chelates essential minerals, binds amino acids and proteins and inhibits digestion enzymes and reduces food's nutritional value.
Monogastric animals did not use phytate-bound phosphorus because there was insufficient phytate degrading activity in their guts. Hydrolysis of phytate can be beneficial for the release of valuable nutrients that can be used and reducing animal phosphorus excretion.
Pseudomonas and Escherichiacoli have been used to isolate phytase. Numerous studies have demonstrated the effectiveness of supplement microbial phytases in increasing the utilization of the phosphate from the phytate.
It has been difficult to find naturally occurring phytases with the required thermostability for animal feed application. The purpose of the study was to identify an alkaline-thermostable phytase derived from Alcaligenes species and evaluate its potential application in in vitro digestion. This study will enhance our understanding of biotechnological applications of phytase to the feed industry.