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Plant Physiol, August 2001, Vol. 126, pp. 1598-1608

A Novel Phytase with Sequence Similarity to Purple Acid Phosphatases Is Expressed in Cotyledons of Germinating Soybean Seedlings 1

Carla E. Hegeman2 and Elizabeth A. Grabau*

Department of Plant Pathology, Physiology, and Weed Science, Fralin Biotechnology Center, Virginia Tech, Blacksburg, Virginia 24061-0346

Phytic acid (myo-inositol hexakisphosphate) is the major storage form of phosphorus in plant seeds. During germination, stored reserves are used as a source of nutrients by the plant seedling. Phytic acid is degraded by the activity of phytases to yield inositol and free phosphate. Due to the lack of phytases in the non-ruminant digestive tract, monogastric animals cannot utilize dietary phytic acid and it is excreted into manure. High phytic acid content in manure results in elevated phosphorus levels in soil and water and accompanying environmental concerns. The use of phytases to degrade seed phytic acid has potential for reducing the negative environmental impact of livestock production. A phytase was purified to electrophoretic homogeneity from cotyledons of germinated soybeans (Glycine max L. Merr.). Peptide sequence data generated from the purified enzyme facilitated the cloning of the phytase sequence (GmPhy) employing a polymerase chain reaction strategy. The introduction of GmPhy into soybean tissue culture resulted in increased phytase activity in transformed cells, which confirmed the identity of the phytase gene. It is surprising that the soybean phytase was unrelated to previously characterized microbial or maize (Zea mays) phytases, which were classified as histidine acid phosphatases. The soybean phytase sequence exhibited a high degree of similarity to purple acid phosphatases, a class of metallophosphoesterases.


1 This work was supported in part by the U.S. Department of Agriculture National Research Initiative Competitive Grants Program.

2 Present address: Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.

* Corresponding author; e-mail egrabau{at}vt.edu; fax 540-231-7126.

© 2001 American Society of Plant Physiologists



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