Korean Journal of Food Science and Technology (한국식품과학회지)

Korean Society of Food Science and Technology (한국식품과학회)
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Purification and Thermal Inactivation of Two Lipoxygenase Isoenzymes from Potato Tubers

감자 Lipoxygenase isozyme의 분리와 열불활성화

  • Kim, Young-Myeong (Department of Food Science and Technology, Seoul National University) ;
  • Lee, Chang-Won (Department of Microbiology, Gyeongsang National University) ;
  • Park, Kwan-Hwa (Department of Food Science and Technology, Seoul National University)
  • Published : 1987.10.01
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Abstract

Two lipoxygenases (F-I and F-II) were purified from potato tubers by ammonium sulfate fractionation and ion-exchange column chromatographies. The purified isoenzymes were apparently homogeneous on polyacrylamide gel electrophoresis. Both enzymes showed a similar optimum pH of 5.5-6.0. From thermal inactivation experiments with the purified enzymes in the range of 50 to $65^{\circ}C$, D-values of 13.3 min and 4.3 min at $65^{\circ}C$, and z-values of $11.8^{\circ}C\;and\;10.3^{\circ}C$ were obtained respectively for F-I and F-II. By applying absolute reaction rate equation, thermodynamic parameters wire also determined for the activation part of the inactivation process.

황산암모늄분획 침전, 이온교환컬럼 크로마토그래프를 이용하여 감자로부터 2개의 Lipoxygenase isozyme(F-I 및 F-II)을 분리정제하고 각각의 isozyme에 대하여 열불활성화 실험을 행하였다. 분리된 isozyme은 polyacrylamide gel 전기 영동상에서 단일밴드를 보였으며 두 isozyme의 최적 pH는 $5.5{\sim}6.0$으로 비슷하였다. 열불활성화 온동 범위인 $50{\sim}60^{\circ}C$에서 F-I 및 F-II의 $D_{65}$값은 각각 13.3min 및 4.3min이었으며 Z 값은 $11.8^{\circ}C$ 및 $10.3^{\circ}C$ 이었다. 또한 각 isozyme의 열역학적인 상수를 절대반응속도식에 따라 구하였다.

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