Purification and Characterization of a Thermostable Catalase from Culture Broth of Thermoascus aurantiacus
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概要
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A thermostable catalase from the culture broth of Thermoascus aurantiacus grown on ethanol was purified as an electrophoretically and isoelectrophoretically homogeneous protein. The molecular weights of the native enzyme and its subnit were estimated to he approximately 330, 000 and 75, 000 by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis, respectively. The enzyme was proven to be a homo-tetrameric hemecatalase with one iron atom per subunit and about 11% carbohydrate. The pI was 4.5. The enzyme was stable up to 80℃ and over a wide range of pH from 5 to 13. The optimum pH was in the range of 6 to 10 and the optimum temperature was 70℃. The K_m and K_<cat> of the enzyme for hydrogen peroxide were 4.8×10^<-2> M and 1.07×10^5 s^<-1> respectively. The enzyme was strongly inhibited by potassium cyanide and sodium azide.
- 公益社団法人日本生物工学会の論文
- 1998-02-25
著者
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Urakami Teizi
Biochemical Division Mitsubishi Gas Chemical Co.
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Shinoyama Hirofumi
Department Of Bioresources Chemistry Faculty Of Horticulture Chiba University
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Shinoyama Hirofumi
Department Of Agricultural Chemistry Chiba University
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Fujii Takaaki
Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University
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WANG HONGXIAN
Department of Bioresources Chemistry, Faculty of Horticulture, Chiba University
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TOKUSIGE YUKIKO
Department of Bioresources Chemistry, Faculty of Horticulture, Chiba University
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Tokusige Yukiko
Department Of Bioresources Chemistry Faculty Of Horticulture Chiba University
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Fujii Takaaki
Department Of Bioresources Chemistry Faculty Of Horticulture Chiba University
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Wang Hongxian
Department Of Bioresources Chemistry Faculty Of Horticulture Chiba University
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FUJII Takaaki
Department of Agricultural Chemistry, Chiba University
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Shinoyama Hirofumi
Department of Advanced Bioresources Science, Graduate School of Science and Technology, Chiba University
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URAKAMI TEIZI
Biochemical Division, Mitsubishi Gas Chemical Co.
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