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enzymatic activity recovery
相关语句
  酶活力恢复
     Calf intestinal alkaline phosphatase (CIP) was denatured in 3 mol/L guanidine hydrochloride solutions for 2 h at 25 ℃. Under suitable renaturation conditions, the kinetic courses of enzymatic activity recovery were investigated in the absence and presence of magnesium ions at 2 mmol/L concentration, and compared to each other.
     在 2 5℃室温下 ,以 3mol/L盐酸胍对小牛肠碱性磷酸酶 (CIP)进行了 2h的去折叠实验 ,然后再以Tris HCl缓冲液对变性体系进行 2 0倍稀释 ,观察该酶活力恢复的动力学过程并与镁离子参与下的稀释复性过程进行比较。
短句来源
  酶活力回收率
     hydrophobic chromatography and Sephadex G-25 Fine. The final specific activity of LDH could beup to 1025.1 U/mg and purity was 88%. 28.7-fold purification was obtained with 67.9%enzymatic activity recovery.
     疏水层析及Sephadex G-25 Fine凝胶过滤等方法进行分离纯化,比酶活达1025.1 U/mg,纯度达88%,纯化倍数达到28.7倍,酶活力回收率为67.9%;
短句来源
     hydrophobic chromatography,and Sephadex G-25 Fine. The final specific activity of LDH was up to 1096.8 U/mg and the purity was 88%. 21.4-fold purification was obtained with enzymatic activity recovery of 53.9%.
     疏水层析及Sephadex G-25 Fine凝胶过滤等方法进行分离纯化,比酶活达1 096.8 U/mg,纯度达88%,纯化倍数达到21.4倍,酶活力回收率为53.9%;
短句来源
  “enzymatic activity recovery”译为未确定词的双语例句
     The activity of immobilized enzyme was 891 U/g, and enzymatic activity recovery reached 359%. 
     制得的固定化酶活力为89 1U/g载体,酶的活力回收达到35 9%.
短句来源
     The specific activity of purified nitrile hydratase reaches 2648.0 Umg-1 and the overall purification fold is 9.42 with an enzymatic activity recovery of 40.84%.
     腈水合酶比酶活达到2648.0U穖g-1,酶活收率为40.84%,用SDS-PAGE检测其纯度为99.00%以上。
短句来源
  相似匹配句对
     Enzymatic Synthesis of Biosurfactants
     酶法合成生物表面活性剂
短句来源
     THE ENZYMATIC PRODUCTION OF D(-)-PHYDROXYPHENYLGLYCINE
     酶法生产D(-)对羟基苯甘氨酸
短句来源
     Recovery factor
     采收率
短句来源
     On the Right of Recovery
     归入权问题之研究
短句来源
     Recovery of "the Other"
     “他者”的复苏
短句来源
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Taking fibroinchitosan blend membranes that contained abundant amino groups as carrier, superoxide dismutase(SOD) extracted from the Tussah pupa was immobilized.The optimal conditions for immobilization of the enzyme were obtained. The optimal conditions were enzyme concentration 38 U/mL, pH 63,temperature 4~8℃ and time 15 h, respectively.The activity of immobilized enzyme was 891 U/g, and enzymatic activity recovery reached 359%.

采用富含自由氨基的丝素 壳聚糖合金膜为载体,吸附固定从柞蚕蛹提取分离的超氧化物歧化酶(SOD),研究并确定了固定化的最佳条件,分别为酶浓度38U/mL、pH6 3、温度4~8℃、时间15h.制得的固定化酶活力为89 1U/g载体,酶的活力回收达到35 9%.

Recently the refolding studies have been concentrated on alkaline phosphatase from E. Coli. The present experiments studied the refolding of mammalian enzyme. Calf intestinal alkaline phosphatase (CIP) was denatured in 3 mol/L guanidine hydrochloride solutions for 2 h at 25 ℃. Under suitable renaturation conditions, the kinetic courses of enzymatic activity recovery were investigated in the absence and presence of magnesium ions at 2 mmol/L concentration, and compared to each other. The two remarkably...

Recently the refolding studies have been concentrated on alkaline phosphatase from E. Coli. The present experiments studied the refolding of mammalian enzyme. Calf intestinal alkaline phosphatase (CIP) was denatured in 3 mol/L guanidine hydrochloride solutions for 2 h at 25 ℃. Under suitable renaturation conditions, the kinetic courses of enzymatic activity recovery were investigated in the absence and presence of magnesium ions at 2 mmol/L concentration, and compared to each other. The two remarkably different courses characterized by the final values of activity recovery, recovery levels, kinetic constants of activity recovery and relative standard deviation of the data indicated that magnesium ions behaved like "site-specific" effectors which were bound to the concerning residues of enzyme protein and stabilized the conformation of active site domain, thus guided the refolding process in a productive pathway.

对小牛肠碱性磷酸酶再折叠的机制及其影响因素进行了探讨。在 2 5℃室温下 ,以 3mol/L盐酸胍对小牛肠碱性磷酸酶 (CIP)进行了 2h的去折叠实验 ,然后再以Tris HCl缓冲液对变性体系进行 2 0倍稀释 ,观察该酶活力恢复的动力学过程并与镁离子参与下的稀释复性过程进行比较。并就不同实验条件下含镁稀释或不含镁稀释 ,获得的最终酶活力、酶活力恢复水平、活力恢复速率常数及数据的相对标准偏差等指标进行了探讨。认为镁是CIP位点的特异性“效应分子” ,它与酶中有关基团的配位 ,稳定了酶活性部位的构象 ,使得自发折叠过程能够向类天然态的方向进行

Nitrile hydratase (NHase), which catalyzes the hydration of nitriles to amides, has been used in industrial production of acrylamide. To obtain the enzymatic properties of NHase from Nocardia sp., the enzyme was purified from cell free extract by ion exchange chromatography and hydrophobic interaction chromatography. The cell ultrasonication time was optimized aiming at the high specific activity of NHase in cell free extract. The procedures of ion exchange chromatography were optimized in terms of pH, ionic...

Nitrile hydratase (NHase), which catalyzes the hydration of nitriles to amides, has been used in industrial production of acrylamide. To obtain the enzymatic properties of NHase from Nocardia sp., the enzyme was purified from cell free extract by ion exchange chromatography and hydrophobic interaction chromatography. The cell ultrasonication time was optimized aiming at the high specific activity of NHase in cell free extract. The procedures of ion exchange chromatography were optimized in terms of pH, ionic strength of buffer and elution volume. The results show that 50mmolL-1 sodium phosphate buffer at pH 7.20 is optimal for equilibration and sampling, and it is most suitable that the sample is eluted with 0.00 to 1.00mmolL-1 NaCl for 20 or 25 times of column volume in a gradient elution. The sample gathered under the optimized condition of ion exchange chromatography was purified by hydrophobic interaction chromatography. The specific activity of purified nitrile hydratase reaches 2648.0 Umg-1 and the overall purification fold is 9.42 with an enzymatic activity recovery of 40.84%. According to the results of SDS-PAGE, the purity of the Nocardia sp. nitrile hydratase purified by HIC is more than 99.00% and the enzyme comprises two subunits, whose molecular weights are 27.38 kDa and 22.90 kDa respectively.

对Nocardiasp.高活力腈水合酶进行了纯化研究。在细胞破碎中,超声时间对腈水合酶比酶活存在一个最优值,超声时间为20.00min时得到的比酶活最高。在离子交换层析过程中,采用DEAE-Sepharose作为层析介质,分别对平衡缓冲液pH、离子强度和线性梯度洗脱体积进行了优化。结果表明,采用pH7.20、50mmolL-1的Na2HPO4-NaH2PO4溶液作为平衡缓冲液,0.00~1.00molL-1的NaCl线性梯度洗脱,洗脱体积为20~25倍柱体积,此条件下腈水合酶的纯化倍数和酶活收率较佳。以Phenyl-SepharoseFF为层析介质研究了疏水层析精制腈水合酶的工艺过程,采用两步层析优化方法纯化出的Nocardiasp.腈水合酶比酶活达到2648.0U穖g-1,酶活收率为40.84%,用SDS-PAGE检测其纯度为99.00%以上。Nocardiasp.腈水合酶的两个亚基分子量分别为22.90kDa和27.38kDa。

 
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