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KMID : 0380619910230040414
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Korean Journal of Food Science and Technology
1991 Volume.23 No. 4 p.414 ~ p.419
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Isolation and Characteristic of Polyphenol Oxidase from Jerusalem Artichoke Tuber
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Abstract
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Polyphenol oxidase from Jerusalem artichoke(Helianthus tuberosus L.) tubers was partially purified by precipitation with ammonium sulfate, followed by gel filtration on Sephadex G-100. The enzyme showed maximal activity at pH 6.5 and 4℃. Kinetic studies indicated Km value of 3 mM for catechol and activation energy of 72.6 ㎉/mole. As for substrate specificity of polyphenol oxidase the enzyme showed high affinity towards diphenol compounds, but not towards monophenols. The enzamatic browning was completely inhibited at 1 mM concentration of L-ascorbic acid, sodium hydrosulfite and L-cystein(HCl). The activity of polyphenol oxidase in 0.1 M potassium phosphate buffer(pH 6.5) was fairly stable for a week at 4℃, while it decreased remarkably at 25℃.
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