Abstract
Two novel phytase genes belonging to the histidine acid phosphatase family were cloned from Yersinia rohdei and Y. pestis and expressed in Pichia pastoris. Both the recombinant phytases had high activity at pH 1.5–6.0 (optimum pH 4.5) with an optimum temperature of 55°C. Compared with the major commercial phytases from Aspergillus niger, Escherichia coli, and a potential commercial phytase from Y. intermedia, the Y. rohdei phytase was more resistant to pepsin, retained more activity under gastric conditions, and released more inorganic phosphorus (two to ten times) from soybean meal under simulated gastric conditions. These superior properties suggest that the Y. rohdei phytase is an attractive additive to animal feed. Our study indicated that, in order to better hydrolyze the phytate and release more inorganic phosphorus in the gastric passage, phytase should have high activity and stability, simultaneously, at low pH and high protease concentration.
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Acknowledgments
This research was supported by the National Basic Research Program of China (973 Program, Grant No. 2004CB719606) and the National High Technology Research and Development Program of China (863 program, Grant No. 2006AA020101). We thank Professor Yang RF and Wang XY of the Academy of Military Medical Sciences for providing genomic DNA of Yersinia spp.
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Huang, H., Luo, H., Wang, Y. et al. A novel phytase from Yersinia rohdei with high phytate hydrolysis activity under low pH and strong pepsin conditions. Appl Microbiol Biotechnol 80, 417–426 (2008). https://doi.org/10.1007/s00253-008-1556-5
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DOI: https://doi.org/10.1007/s00253-008-1556-5