Journal of the Korean Society of Food Science and Nutrition (한국식품영양과학회지)

The Korean Society of Food Science and Nutrition (한국식품영양과학회)
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Purification and Some Properties of Peroxidase from the Fruit Malus sieboldii (Regel) Rehder

아그배 Peroxidase의 정제 및 특성

  • Yang, Hee-Cheon (Dept. of Food Science and Technology, Jeonju Woosuk University) ;
  • Son, Hee-Suk (Dept. of Home Economics, Chonbuk National University) ;
  • Shim, Kyu-Kwang (Dept. of Biotechnology, Jeonju Woosuk University) ;
  • Oh, Chan-Ho (Dept. of Biotechnology, Jeonju Woosuk University) ;
  • Choi, Dong-Seong (Dept. of Biotechnology, Jeonju Woosuk University)
  • 양희천 (전주우석대학 식품공학과) ;
  • 손희숙 (전북대학교 가정교육학과) ;
  • 심규광 (전주우석대학 생물공학과) ;
  • 오찬호 (전주우석대학 생물공학과) ;
  • 최동성 (전주우석대학 생물공학과)
  • Published : 1992.03.01
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Abstract

Peroxidase in the fruit of Malus sieboldii (Regel) Rehder was partially purified by DEAE-cellulose column chromatography and Ultro-AcA 54 gel filtration. The optimum pH of peroxidase was 4.5 and optimum temperature was $80^{\circ}C$. The enzyme was stable at pH 5.0 and below $30^{\circ}C$, and inactivated by heat treatment at $80^{\circ}C$ for 15min. In the presence of 30mM $H_{2}O_2$ Km value on o-phenylenediamine as substrate was 1.65mM, and in the presence of 10mM o-phenylenediamine Km value on $H_{2}O_2$ was 7.97mM. L-Ascorbic acid and sodium L-ascorbate greatly inhibited the enzyme activity and among several metal ions $Mn^{2+}$ only increased the activity at 5mM.

아그배로 부터 아세톤 침전, DEAE-cellulose 칼럼 크로마토그라피, Ultro-AcA 54겔여과의 과정을 거쳐 peroxidase를 분리 정제하고, 그의 특성을 조사하였다. 아그배peroxidase의 반응 최적 pH는 4.5, 반응최적 온도는 $80^{\circ}C$이었고, $30^{\circ}C$ 이하의 온도와 pH 5.0에서 안정하였으며, $80^{\circ}C$에서 15분간 보존했을 때 거의 불활성화되었다. OPDA에 높은 활성을 나타내었으나, phenol류 기질에 대해서는 약간의 활성을 나타내었으며, OPDA와 $H_{2}O_2$에 대한 Km치는 각각 1.65mM, 7.97mM이었다. 아그배 peroxidase에 대한 저해작용은 L-ascorbic acid와 sodium L-ascorbate가 가장 컸고, 금속이온 중 $Mn^{2+}$만이 5mM 농도에서 효소의 활성을 증가시켰다.

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