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제주산 키위에서 분리한 단백질분해효소 Actinidin 의 정제 및 특성 KCI 등재

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한국식품영양학회지 (The Korean Journal of Food And Nutrition)
한국식품영양학회 (The Korean Society of Food and Nutrition)
초록

제주산 키위에서 추출 정제한 단백분해효소의 특성을 조사하였다. 본 효소는 DEAE-Toyopearl 650C, Sephadex G-100 chromatography에 의해 정제하였고 비활성은 8.5배 증가하고 회수율은 25%이었다. 이 효소는 40℃, pH 7에서 최대활성을 나타내었으며 30∼50℃, pH 5.0∼9.0사이에서 안정하고 K_m값은 32 mM, 분자량은 27, 000으로 추정된다. Hg^+, Co^2- 이온에 의해 활성이 저해되며 phenylmercuric acetate, leupeptin에 의해 저해되므로 활성부위에 thiol기를 갖는 것으로 추정되어진다.

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 Sephadex 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 40℃, respectively. This enzyme was stable at the ranges of pH 5.0∼9.0 and below 50℃. It was also found that Fe^+2, Fe^+3, and Na^+ ions increased the 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 enzyme had thiol-group. The enzyme reaction followed the Michaelis-Menten kinetics with the K_m value of 0.32 mM for casein.

저자
  • 김명희 | Myung Hee Kim
  • 최미경 | Mi Kyeong Choi
  • 김미원 | Mi Won Kim
  • 전예숙 | Ye Sook Jeon
  • 김미선 | Mi Sun Kim