Soybean peroxidase의 추출공정 및 안정성 특성

Extraction Process and Stability Characteristics of Soybean Peroxidase

  • 서경림 (한양대학교 화학공학과 생물공정연구실) ;
  • 이은규 (한양대학교 화학공학과 생물공정연구실)
  • 발행 : 1998.10.01

초록

Soybean peroxidase was extracted from soybean hulls and purified by ammonium sulfate precipitations (25% and 75% saturation), pl fractionation, and anionic exchange and gel filtration chromatographies (DEAE-Sephadex A-50 and Superose 12). Modlecular weight and pl value were estimated to be ca. 45 kD and 4.2, respectively. Purified soybean peroxidase had an RZ value of 0.43. Compared with horseradish peroxidase, it showed superior thermal and pH stability. Assuming the first-order kinetics, the thermal deactivation rate constant of soybean peroxidase at 80$^{\circ}C$ was about 8 times lower than that of horseradish peroxidase. Deactivation energy was calculated to be 69.3 kcal/mol. Soybean peroxidase showed about 10% higher H2O2 degradation capacity than horseradish peroxidase. Exploiting these advantages, the soybean peroxidase purified from the domestic soybean hull is expected to replace horseradish peroxidase in various applications.

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