Partial Purification and Some Properties of Polyphenol Oxidase from Aster scaber

참취로부터 추출한 Polyphenol Oxidase의 부분정제 및 성질

A polyphenol oxidase from the crude extract of Aster scaber was partially purified by (NH4)2 SO4 precipitation and subsequent Sephadex G-150 chromatography. The final preparation showed five peaks of enzyme activity. Optimum pH and temperature for the activity of polyphenol oxidase were 7.0 and $30^{\circ}C$, respectively. Enzyme activity was stable at $40^{\circ}C$ for 5min in pH 7.0 reaction mixture but ceased completely at $60^{\circ}C$ for 30min and $70^{\circ}C$ for 5min at pH 7.0. The olyphenol oxidase has good activity acid but was inactive on DL-depa. The apparent Km for catechol was about 17.6mM.

참취로부터 추출한 poluphenol oxidase의 부분정제를 $(NH_4)_2SO_4$ 처리 및 Sephadex G-150 column chromatogaphy에 의해 분리하였다. Polypenol oxidase의 최적pH와 최적온도는 각각 7.0과 $30^{\circ}C$였으며, 효소활성은 $60^{\circ}C$에서 30분간 처리시와 $70^{\circ}C$에서 5분간 처리시 완전실활하였다. 기질특이성에서는 chlorogenic acid의 기질이 높은 특이성을 나타난 반면 DL-dopa는 활성을 억제하였다. Polyphenol oxidase의 Km값은 17.6mM이었다.