The Korean Journal of Food And Nutrition (한국식품영양학회지)

The Korean Society of Food and Nutrition (한국식품영양학회)
권호 표지

Purification and Characterization of a Pretense Actinidin Isolated from Cheju Kiwifruit

제주산 키위에서 분리한 단백질분해효소 Actinidin의 정제 및 특성

  • 조성자 (고려대학교 식품공학과) ;
  • 정수현 (고려대학교 식품공학과, 고려대학교 병설보건전문대학 식품영양과, 경기대학교 식품가공학과, 순천향대학교 사회체육과, 고려대학교 식품공학과)
  • Published : 1994.06.01
Download PDF
⟨ Previous Next ⟩

Abstract

A protease, actinidin, was isolated from Cheju kiwi fruit Actinidia chinesis. The enzyme was purified about 8.5 fold with the yield of 25% by column chromatographies of DEAE-Toyopearl and Sphadex. G-100. Purified enzyme gave a single protein band on polyacrylamide gel electrophoresis and its molecular weight estimated by SDS-PAGE was about 27, 000. The optimum pH and temperature were 7.0 and 4$0^{\circ}C$, respectively. This enzyme was stable at the ranges of pH 5.0~9.0 and below 5$0^{\circ}C$. It was also found that Fe+2, Fe+3, and Na+ ions increased enzyme activity, whereas Hg+2 and Co+2 ions decreased. The enzyme was inhibited by phenylmercuric acetate and leupeptin, which indicated that active center of the emzyme had thiol-group. The enzyme reaction followed the Michaelis-Men-ten dkinetics with the Km value of 0.32 mM for casein.

Keywords