Purification and Charancterization of Glutamate Decarboxylase from Aspergillus oryzae

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概要

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• We purified glutamate decarboxylase (GAD) [EC4.1.1.15] from Aspergillus oryzae and characterized its biochemical and kinetic properties. GAD was purified by ammonium sulfate at 30–70% saturation and chromatographies on Sephacryl S-300, DEAE-FF and CM-FF. The purification of GAD from the crude enzyme solution was 40-fold and the recovery rate was 4.9%. About 230 μg of purified enzyme was obtained from 20 g of the mycelia of A. oryzae. The purified preparation of the enzyme showed a single protein band on SDS-PAGE. The molecular weight of purified GAD by SDS-PAGE and gel filtration was estimated to be 48 kDa and 300 kDa, respectively, suggesting that purified GAD had a hexameric structure. The Km value for L-glutamic acid, a substrate of the enzyme, was estimated to be 13 mM. The optimum pH and temperature of GAD were 5.5 and 60°C, respectively. The GAD activity was stable up to 40°C.

• 社団法人　日本食品科学工学会の論文
• 2003-08-01

著者

• NISHIMURA KENRYO

  Kumamoto Industrial Research Institute

• TSUCHIYA Kimi

  Kumamoto Industrial Research Institute

• IWAHARA Masayoshi

  Sojo University

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• Purification and Charancterization of Glutamate Decarboxylase from Aspergillus oryzae

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