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KMID : 1025520090510020177
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Journal of Animal Science and Technology
2009 Volume.51 No. 2 p.177 ~ p.182
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General Enzymatic Properties of Human Histidine Acid Phosphatase-Phytase
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Cho Jaie-Soon
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Abstract
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The glycosylated human MINPP(multiple inositol polyphosphate phosphatase), which was recombinantly over-expressed by using industrial host, Pichia pastoris, showed the phytase activity against phytate(InsP6) and the enzyme activity of the unglycosylated counterpart was decreased to 30%. The optimal phytase activity occurred at pH 7.4. The human MINPP showed high substrate specificity for InsP6 with little activity on other organic phosphate conjugates such as para-nitrophenylphosphate(pNPP), ATP, and ribose-1-phosphate(R-1-P). The phosphatase activity against 2,3-bisphosphoglycerate(2,3-BPG) by human MINPP was increased to 1.2-fold in the presence of stimulator, 1mM 2-phosphoglycolate(2-PG) but the phytase activity against InsP6 was not affected by addition of 1mM 2-PG. The phosphatase activity against 2,3-BPG by human MINPP was not increased in the presence of 2 mM Mg2+ or 100mM Cl－.
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KEYWORD
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MINPP, pichia pastoris, phytase, phosphatase
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