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題名 | 白蝦(Litopenaues vannamei)肝胰臟鹼性磷酸酯酶之研究=A Study on the Activity of Alkaline Phosphatase from Hepatopancreas of White Shrimp (Litopenaeus vannamei) |
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作者 | 陳均全; 黃獻龍; 李安進; Chen, Chun-Chuan; Huang, Shiang-long; Lee, An-Chin; |
期刊 | 中華生質能源學會會誌 |
出版日期 | 20041200 |
卷期 | 23:3/4 民93.12 |
頁次 | 頁69-78 |
分類號 | 387.13 |
語文 | chi |
關鍵詞 | 鹼性磷酸酯酶; 溫度; Ph值; 白蝦; Alkaline phosphatase; Temperature; Ph; White shrimp; |
中文摘要 | 白蝦肝胰臟鹼性磷酸酯酶經由粗萃取、正丁醇粹取、酸化處理(pH4.8)、離子交換管柱(DEAE, pH7.6)、離子交換管柱(DATE, pH5.5)和膠過濾管柱等步驟,其比活性分別為25.4,32.7,28.6,53.2,998和1670 unit/mg,經過這些步驟後,其純度提高66倍。探討溫度、酸鹼度、鎂離子、鋅離子和抑制劑對鹼性磷酸酯酶活性的影響,發現此鹼性磷酸酯酶最適的pH值為8.5,最適的溫度為45℃;在熱穩定性方面,酵素經56℃熱處理5分鐘後,酵素活性僅殘留63%;酵素對p-nitrophenyl phosphate的KM為0.46mM,Vmax為2130U./mg;100mM的鎂離子可活化酵素活性153%;10µM的鋅離子可活化酵素活性120%,然而100µM的鋅離子對酵素卻有抑制的作用,其活性僅為控制組的70%;EDTA對酵素的活性亦具有抑制作用,在1mM時可抑制酵素活性63%。 |
英文摘要 | The alkaline phosphatase from hepatopancreases of white shrimp was isolated by crude extraction, by n-butanol extraction, by acidification, by ion-exchange chromatography (pH7.6), by ion-exchange chromatography (pH5.5) and by gel filtration. The specific activitites of the isolated enzymes just after each of those steps were 25.4, 32.9, 28.6, 53.2, 998 and 1670 unit/mg, respectively. The purity of the isolated enzymes was increased by a factor of 66 after the isolation of those steps. The approach of the effect of temperature, pH, magnesium ions, zinc ions and inhibitors on the activity of alkaline phosphatase was conducted. The optimal pH and temperature of the enzyme were found to be 8.5 and 45℃, respectively. The 63% of activity was remained after 56℃ pretreatment for 5 minutes. The KM and Vmax of alkaline phosphatases for p-nitrophenyl phosphate was observed to be 0.46 mM and 2130 unit/mg, respectively. The 153% and 120% of enzyme activities were activated by the addition of 100 mM fo magnesium ions and 10µM of zinc ions, respectively. However, a hundred of micromolar of zinc ions exerts an inhibitory effect on the enzyme activity (70% enzyme activity remaining). EDTA has also an inhibitory effect on the enzyme activity. Its residual acitvity was 63% in the presence of 1 mM of EDTA. |
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