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Bioresour Technol. 2010 Jun;101(11):4125-31. doi: 10.1016/j.biortech.2010.01.001. Epub 2010 Feb 9.

Purification, characterization, and cloning of a novel phytase with low pH optimum and strong proteolysis resistance from Aspergillus ficuum NTG-23.

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  • 1State Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, China.


A novel phytase was isolated from Aspergillus ficuum NTG-23 with a procedure involving ion-exchange chromatography on DEAE-cellulose, CM-cellulose and FPLC-gel filtration on Superdex 75. The protein exhibited a molecular mass of 65.5kDa in gel filtration and SDS-PAGE. It possessed an optimal pH of 1.3 and an optimal temperature of 67 degrees C, and manifested a K(m) of 0.295mM and a V(max) of 55.9nmol (phosphate)/min. Phytase activity was not significantly affected by metal ions such as Ca(2+), Mg(2+), Mn(2+), Zn(2+), but was slightly stimulated in the presence of EDTA. The phytase was stable at 60 degrees C with no obvious loss of activity upon its incubation at 70 degrees C for 20min. The enzyme exhibited a broad substrate selectivity and showed strong resistance toward pepsin and trypsin. The unique properties suggest that the phytase has the potential to be useful as an animal feed supplement.

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