Purification and Characterization of Phytase Induced in Tomato Roots under Phosphorus-Deficient Conditions
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概要
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Phytase (myo-inositol hexakisphosphate phosphohydrolase; EC 3.1.3.8) was purified from roots of tomato plants grown under phosphorus-deficient conditions using five purification schemes. The phytase was successfully separated from the major acid phosphatase to an electrophoretic homogeneity. The native molecular weight of this enzyme was estimated to be about 164 kD by Bio-Gel P-200 gel filtration. The molecular weight of the subunit on SDSPAGE was approximately 82 kD, indicating that the native form of the enzyme was a homodimer. The isoelectric point of tomato phytase was about 5.5. The enzyme exhibited a high affinity for phytie acid (K_m=38 μM), and was strongly inhibited by phosphate, molybdate and fluoride. Among other characteristics of tomato phytase, the pH and temperature optima were 4.3 and 45℃, respectively. Tomato phytase contained a fairly high concentration of aspattic, glutamic acid and glyeine residues.
- 社団法人日本土壌肥料学会の論文
著者
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Osaki Mitsuru
Faculty of Agriculture, Hokkaido University
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Tadano Toshiaki
Faculty of Agriculture, Hokkaido University
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Osaki Mitsuru
Faculty Of Agriculture Hokkaido University
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HONMA Mamoru
Faculty of Agriculture, Hokkaido University
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Tadano Toshiaki
Faculty Of Agriculture Hokkaido University
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Honma M
Department Of Applied Bioscience Graduate School Of Agriculture Hokkaido University
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Honma Mamoru
Faculty Of Agriculture Hokkaido University
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Li Minggang
Faculty of Agriculture, Hokkaido University
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Li Minggang
Faculty Of Agriculture Hokkaido University
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