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KMID : 0380019940090010055
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Korean Journal of Biotechnology and Bioengineering
1994 Volume.9 No. 1 p.55 ~ p.61
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Novel purification and Characterization of Glucose oxidase Aspergillus niger
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한상배/Han, Sagn Bae
김광진/임한진/김태년/최동성/Kim, Kwang Jin/Lim, Han jin/Kim, Tae Nyeon/Choi, Dong Seong
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Abstract
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Glucose oxidase( EC 1.1.3.4) was purified to electrophoretic homogeneity from Aspergillus niger by a combination of ammonium sulfate fractionation, ion exchange chromatography, and ultrafiltration. Two active fractions, A and B, of glucose oxidase were obtained from the hydrophobic chromatography on phenyl sepharose CL-4B. The enzyme A and B were glycoproteins with the same denatured molecular weight of 78,000 and had specific activities of 2,191 and 1,273 units/mg protein, respectively. But the two enzymes showed differences in native molecular weight which was measured by HPLC gel filteration, maximum absorbtion wavelength, and isoelectric point. The enzyme A oxidized ~--D-glucose only and was resistant to sodium dodecyl sulfate. Activity optimum was found at 301C and pH 3.5. Also the enzyme A was inhibited greatly by Hg2+(10mM). The results of chemical modification experiments suggested that cysteine and cystine residues might be involved in the active site of the enzyme A.
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