A Calcium-Activated Phytase from Pollen of Lilium longiflorum
Open Access
- 1 September 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 82 (1) , 333-335
- https://doi.org/10.1104/pp.82.1.333
Abstract
A phytase was isolated and partially purified from the pollen of Lilium longiflorum Thumb. Optimum activity was at pH 8.0. The phytase was activated by Ca2+ and Sr2+ but not by the other divalent cations tested. Activity was inhibited by ethylenediaminetetraacetate. The phytase had a temperature optimum of 55 to 60°C and an activation energy of about 12,700 calories/mole. Extraction of L. longiflorum pollen with 0.1% Triton X-100 increased recovery of the phytase by nearly 4-fold. The phytase had a molecular weight of about 88,000 as determined by gel filtration chromatography and a Km value of 7.2 micromolar for phytic acid in the presence of Ca2+.Keywords
This publication has 8 references indexed in Scilit:
- A New Type of Phytase from Pollen ofTypha latifoliaL.Agricultural and Biological Chemistry, 1985
- Polyphosphoinositides are present in plant tissue culture cellsBiochemical and Biophysical Research Communications, 1985
- The Polyphosphoinositides RevisitedScience, 1985
- Phytate metabolism in Petunia pollenPhytochemistry, 1984
- myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb.Plant Physiology, 1982
- Phytic acid in pollenPhytochemistry, 1982
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- [10] Assay of inorganic phosphate, total phosphate and phosphatasesPublished by Elsevier ,1966