The effectiveness of an Escherichia coli phytase in improving phosphorus and calcium bioavailabilities in poultry and young pigs

Citation
Fa. Igbasan et al., The effectiveness of an Escherichia coli phytase in improving phosphorus and calcium bioavailabilities in poultry and young pigs, ARCH ANIM N, 54(2), 2001, pp. 117-126
Citations number
19
Categorie Soggetti
Animal Sciences
Journal title
ARCHIVES OF ANIMAL NUTRITION-ARCHIV FUR TIERERNAHRUNG
ISSN journal
0003942X → ACNP
Volume
54
Issue
2
Year of publication
2001
Pages
117 - 126
Database
ISI
SICI code
0003-942X(2001)54:2<117:TEOAEC>2.0.ZU;2-X
Abstract
The effectiveness of an Escherichia coli phytase in comparison with a comme rcially available Aspergillus phytase in improving the bioavailability of p hosphorus in broilers, layers and young pigs was studied in three separate experiments. Three basal diets, marginally deficient in dietary P mainly pr ovided as phytate, were formulated. Both phytases were added to the diets a t the rate of 500 U/kg diet. The phytases significantly (P less than or equ al to 0.05) improved the availability of phytate P to broilers, layers and young pigs. Aspergillus and E. coli phytases enhanced the pre-caecal digest ibility of P by 11 and 29% for broilers and 18 and 25% for layers, respecti vely. 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 co nditions of this study, it was observed that E. coli consistently, though w ith small magnitude in layers and pigs, enhanced the availability of phytat e P at the same range or slightly better than Aspergillus phytase. It was o nly in pigs that the availability of Ca was significantly (P less than or e qual to 0.05) improved by addition of both phytases. It can be concluded th at 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.