Studies of Characteristics of Polyphenol Oxidase in Yan and Antimutagenic effect of Enzymatic Browning Reaction Products

마의 Polyphenol oxidase의 특성과 효소갈변생성물의 항돌연변이 효과

  • Jeong, Seung-Hee (Department of Food and Nutrition, Kyunghee University) ;
  • Lee, Im-Sun (Department of Food and Nutrition, Kyunghee University) ;
  • Koo, Sung-Ja (Department of Food and Nutrition, Kyunghee University)
  • 정승희 (경희대학교 식품영양학과) ;
  • 이임선 (경희대학교 식품영양학과) ;
  • 구성자 (경희대학교 식품영양학과)
  • Published : 1994.11.01

Abstract

Polyphenol oxidase in Yam was partially purified through ammonium sulfate fractionation, DEAE-cellulose column chromatography. The specific activity of purified PPO was 138.22 unit/mg protein. The optimum pH and temperature of purified PPO were respectively 7.0 and 30$^{\circ}C$. The heat treatment at 80$^{\circ}C$ for 6 min, decreased PPO activity to 50%. The enzyme showed high substrate specificity toward catechol. The Km value for catechol was 5 mM. In the Ames test using S. typhimurium TA98 and TA100 catechol-YEBRP, pyrogallol-YEBRP, chlorogenic-YEBRP showed strong antimutagenicity on sodium azide and MECF excepting hydroquinone-YEBRP showed killing effect on both strains.

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