초록

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Abstract ▼ AI-Helper

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 $4^{\circ}C$. Kinetic studies indicated $K_{m}$

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 $4^{\circ}C$. Kinetic studies indicated $K_{m}$ value of 3 mM for catechol and activation energy of 72.6 kcal/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 $4^{\circ}C$, while it decreased remarkably at $25^{\circ}C$.

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