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題名 | Purification and Characterization of Extracellular Lipase from Acinetobacter Radioresistens CMC-2=Acinetobacter Radioresistens CMC-2菌體外脂肪酵素之純化及特性分析 |
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作者 | 吳意珣; 蔡少偉; 陳樹人; Ng, I-son; Tsai, Shau-wei; Chen, Shu-jen; |
期刊 | Journal of the Chinese Institute of Chemical Engineers |
出版日期 | 19990900 |
卷期 | 30:5 1999.09[民88.09] |
頁次 | 頁355-362 |
分類號 | 460.02 |
語文 | eng |
關鍵詞 | 菌體外脂肪酵素; 純化; Alkaline and thermostable lipase; Purification and characterization; Acinetobacter radioresistens; |
中文摘要 | 自Acinetobacter radioresistens CMC-2可生產具有耐熱性以及耐溫性之菌體外 脂肪酵素。經過離心、超過濾及冷凍真空操作,可回收49.5%總活性之粗酵素,再經過 進一步之親油性管柱層析及超過濾操作, 可回收26.6%總活性之純化酵素。 以 SDS-PAGE 及 IEF 分析,獲得脂肪酵素之分子量及等電點分別為 38kDa 與 4.5。 文中除了 探討 pH 值、溫度、金屬離子、界面活性劑及有機溶劑對酵素活性與穩定性影響外,並發現 本酵素對三酸甘油酯具1,3位置選擇性,以及對外消旋 suprofen 三氟乙基酯具(R)- 形立體異構物選擇性。 |
英文摘要 | A novel lipase with the favorable alkaline and thermostable characteristics was produced from Acinetobacter radioresistens CMC-2. The curde lipase with 49.5% of total activity was recovered after centrifugation, ultrafiltration and lyophilization. The crude preparation was further purified to a homogeneous state by column chromatography on phenyl sepharose and ultrafiltration, giving 26.6% of total activity recovery. The molecular weight and isoelectric point of the lipase determined by SDS-PAGE and IEF were 38 kDa and 4.5, respectively. The lipase could be classified as a 1,3-positional specific enzyme and possessed the (R)-stereoselectivity in the hydrolysis of racemic suprofen trifluoroethyl ester in isooctane. Moreover, effects of pH, temperature, metal ions, surfactants and organic solvents on the enzyme activity and stability were reported. |
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