Purification and characterization of mannose isomerase from Agrobacterium radiobacter M-1 |
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Authors: | Hirose J Maeda K Yokoi H Takasaki Y |
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Affiliation: | Department of Applied Chemistry, Faculty of Engineering, Miyazaki University, Japan. jhirose@cc.miyazaki-u.ac.jp |
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Abstract: | A mannose isomerase from Agrobacterium radiobacter M-1 (formerly Pseudomonas sp. MI) was purified to electrophoretic homogeneity and characterized. A cell-free extract was separated by ammonium sulfate fractionation, Butyl-Toyopearl 650M, DEAE-Sepharose and hydroxylapatite column chromatography. Its molecular mass was estimated to be 44 kDa by SDS-PAGE and 90 kDa by gel filtration, in which the enzyme is most likely a dimer composed of two identical subunits. The purified enzyme had an optimum pH at 8.0, an optimum temperature at 60 degrees C, a pI of 5.2 and a Km of 20 mM, and specifically converted D-mannose and D-lyxose to ketose. The N-terminal amino acid sequence was identified. |
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