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- W2033447505 abstract "The gene (phyA) for the Aspergillus niger phytase with optima at pH 5.5 and 2.2 was expressed in Escherichia coli under the control of the T7lac promoter. A 56 kDa fusion protein comprised of phytase linked to an S-Tag leader peptide accumulated in inclusion bodies at 30 °C. The yield of unglycosylated recombinant phytase purified from 50 mL cultures by anion exchange chromatography of solubilized inclusion body protein was 10 mg. The refolded enzyme had an activity of 1.5 μmol mg-1 min-1 at 37 °C, but most of the protein was in the form of inactive aggregates. Recombinant phytase displayed a single pH optimum at pH 5.1, was irreversibly denatured at pH 2.0 and was not active above 55 °C. As with A. niger phytase, the initial breakdown product observed was inositol 1,2,4,5,6-pentakis(phosphate). Km values for the hydrolysis of inositol hexakis(phosphate) and p-nitrophenylphosphate were 96 μM and 2.0 mM, respectively, at pH 4.5. Keywords: Phytase; phosphatase; phytic acid; inositol phosphates; Aspergillus ..." @default.
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- W2033447505 date "1997-08-01" @default.
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- W2033447505 title "Expression of an <i>Aspergillus niger</i> Phytase (<i>phyA</i>) in <i>Escherichia coli</i>" @default.
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- W2033447505 doi "https://doi.org/10.1021/jf970276z" @default.
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