1. The effectiveness of an Escherichia coli phytase in improving phosphorus and calcium bioavailabilities in poultry and young pigs
- Author
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K. Männer, Ortwin Simon, F. A. Igbasan, and G. Miksch
- Subjects
Male ,Swine ,chemistry.chemical_element ,Biological Availability ,Calcium ,Biology ,medicine.disease_cause ,Microbiology ,Small magnitude ,Random Allocation ,medicine ,Escherichia coli ,Animals ,Food science ,Aspergillus ,6-Phytase ,Phosphorus ,biology.organism_classification ,Bioavailability ,Calcium, Dietary ,chemistry ,Phosphorus, Dietary ,Animal Science and Zoology ,Phytase ,Digestion ,Female ,Chickens - Abstract
The effectiveness of an Escherichia coli phytase in comparison with a commercially available Aspergillus phytase in improving the bioavailability of phosphorus in broilers, layers and young pigs was studied in three separate experiments. Three basal diets, marginally deficient in dietary P mainly provided as phytate, were formulated. Both phytases were added to the diets at the rate of 500 U/kg diet. The phytases significantly (Por = 0.05) improved the availability of phytate P to broilers, layers and young pigs. Aspergillus and E. coli phytases enhanced the pre-caecal digestibility of P by 11 and 29% for broilers and 18 and 25% for layers, respectively. Total tract digestibility of P (P balance) was also enhanced but with smaller magnitude. In pigs, total tract digestibility of P was improved by 33 and 34% by Aspergillus and E. coli phytases, respectively. Under the conditions of this study, it was observed that E. coli consistently, though with small magnitude in layers and pigs, enhanced the availability of phytate P at the same range or slightly better than Aspergillus phytase. It was only in pigs that the availability of Ca was significantly (Por = 0.05) improved by addition of both phytases. It can be concluded that E. coli phytase is highly effective in improving the bioavailability of phytate P to broilers, layers and young pigs. This seems to be based on the high proteolytic stability of the enzyme in the digestive tract, as shown recently.
- Published
- 2002