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KMID : 0380619870190050397
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Korean Journal of Food Science and Technology
1987 Volume.19 No. 5 p.397 ~ p.402
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Purification and Thermal Inactivation of Two Lipoxygenase Isoenzymes from Potato Tubers
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Kang Nam-Jun
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Abstract
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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℃, D- values of 13.3 min and 4.3 min at 65℃, and z-values of 11.8℃ and 10.3℃ were obtained respectively for F-I and F-II. By applying absolute reaction rate equation, thermodynamic parameters were also determined for the activation part of the inactivation process.
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