首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Purification, biochemical characterization and antioxidant property of ZCPG, a cysteine protease from Zingiber montanum rhizome
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Purification, biochemical characterization and antioxidant property of ZCPG, a cysteine protease from Zingiber montanum rhizome

机译:ZCPG的纯化,生化表征和抗氧化性能,来自 Zingiber Montanum 根茎

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Highlights?ZCPG was purified to homogeneity to sixteen fold with a total activity of 39.4U/mg.?HPLC chromatogram presented a prominent sharp peak.?SDS-PAGE resolved into ~24.3 and ~24.6kDa subunits indicating the heterodimeric nature.?The pH and temperature optimum were 9 and 60°C whileKm andVmax were 0.5±0.03μg and 13.73±2.07U/ml respectively.?It exhibited strong antioxidant activity and can be effective in therapeutic and food applications.AbstractZingiber montanumcysteine protease glycoprotein (ZCPG) was purified to homogeneity by DEAE- cellulose and Sephadex G50 resulting in sixteen fold purification and total activity of 39.4U/mg. ZCPG presented a prominent single peak in HPLC chromatogram with an estimated molecular
机译:<![CDATA [ 亮点 ZCPG被纯化至均质至16用的39.4U / mg的总活性折叠 HPLC色谱呈现突出的尖锐峰。 <?CE:对ID = “par0015” 视图=”所有 “> SDS-PAGE解析到〜24.3和〜24.6kDa亚单位表示的异二聚体性质 pH和最适温度分别为9和60℃,同时ķ m和 V max分别为0.5±0.03μg和13.73±2.07U / ml的分别 它表现出很强的抗氧化活性,能有效地治疗性和食品应用 < / CE:抽象> 抽象 姜montanum 半胱氨酸蛋白酶糖蛋白(ZCPG)通过DEAE-纤维素和Sephadex G50纯化至均一导致16倍的纯化和39.4U / mg总活性。 ZCPG呈现在HPLC色谱图的一个突​​出的单峰,估计分子

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