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KMID : 0545120040140051004
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Journal of Microbiology and Biotechnology
2004 Volume.14 No. 5 p.1004 ~ p.1008
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Purification and Properties of an Extracellular Acid Phytase from Pseudomonas fragi Y9451
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In MJ
Jang ES/Kim YJ/Oh NS
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Abstract
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An extracellular acid phytase from Pseudomonas fragi Y9451 was purified to homogeneity from the culture supernatant by salting-out DEAE-Sepharose column chromatography CM-Sepharose column chromatography and Sephacryl S-300 gel filtration. The molecular weight of the purified enzyme was estimated to be 74 kDa on gel filtration and 54 kDa and 25 kDa on SDS-PAGE suggesting that the native enzyme was a heterodimeric protein. The purified enzyme was most active at pH 4.5 and 70oC and fairly stable from pH 4.0- 6.0. It was specific for phytate and exhibited a Km value of 27 mM (sodium phytate pH 4.5 50oC). The phytase activity was strongly inhibited (at maximum by 87%) by Fe3+ Cu2+ Fe2+ and Zn2+ at 5 mM concentration and greatly inhibited by Ca2+ at 10 mM concentration. However EDTA notably stimulated the phytase activity at 10 mM concentration. With optimum pH and stability Pseudomonas fragi phytase could be a potential candidate for animal feed applications.
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