Purification and Characterristics of Intercellular Nitrite Oxidase in <i>Pichia angusta</i> Y-11393

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  • <i>Pichia angusta</i> Y-11393株のnitrite oxidaseの精製とその性質
  • Pichia angusta Y-11393株のnitrite oxidaseの精製とその性質
  • Pichia angusta Y-11393カブ ノ nitrite oxidase ノ セイセイ ト ソノ セイシツ

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Nitrite oxidase of Pichia angusta Y-11393 is an intercellular enzyme induced by nitrite in the medium. The enzyme had the highest activity at the early logarithmic growth phase, and the activity decreased gradually. The extracted enzyme was precipitated by each chromatography system. The purified enzyme was a 54.0kDa, monomer protein. The optimum pH was 5.0 and optimum temperature was 50°C. The enzyme had pH stability between pH 4.0 and 7.0; 70% of the enzyme survived at pH3.0 buffer. The enzyme also had thermo-tolerance between 15 and 50°C. This enzyme was inactivated by Fe2+, iodo acetate, Hg2+, EDTA, Sodium azid, NEM (N-ethyl-maleimide) and DTT (Ditiothreitol). It was considered that Cystein was contained in the active site in this enzyme. The Michaelis-Menten constant of nitrite oxidase was as follows; km = 473μM and Vmax = 2.7pM against nitrite, km = 181μM, and Vmax = 26.8 pM against oxygen. Therefore, the reaction of this enzyme depended on oxygen in the substrate. It is considered that the nitrite is a new type in a few reports, and it is an important enzyme for KIMOTO production in sake brewing.

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