Purification and Properties of the Phytase from Schwanniomyces castellii

概要

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Phytase from Schwanniomyces castellii was purified by anion exchange and gel filtration chromatography. The enzyme has a molecular weight of 490,000 with a glycosylation rate around 31%. The structure of the deglycosylated protein is tetrameric, with one large subunit (MW 125,000) and three identical small subunits (MW 70,000). The enzyme exhibits an uncommon preference for high temperature, with optimum activity at 77℃ and thermostability up to 74℃. The optimum pH is 4.4. Phytate is completely dephosphorylated by the phytase and the K_m is 38 μM.
社団法人日本生物工学会の論文
1992-07-25