원문정보
Extraction Process and Stability Characteristics of Soybean Peroxidase
초록
영어
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℃ 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.
목차
재료 및 방법
실험재료
실험기기
SBP 추출 및 정제 공정
정제된 SBP의 분자량, pH 및 RZ 값 측정
SBP와 HRP의 열 및 pH 안정성 평가
SBP 및 HRP의 관산화수소 분해능 평가
결과 및 고찰
SBP 추출 및 정제 공정
SBP의 열 및 pH 안정성
SBP의 과산화수소 분해 능력
요약
감사
참고문헌