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activity recovery     
相关语句
  活力回收
     The result was 347.09U ACE was obtained from 200g hog lung tissue with specific activity 29.029U/mg and activity recovery12.53%.
     200g猪肺可制备出ACE347.09U,比活力29.029U/mg,活力回收12.53%。
短句来源
     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 results of the experiment demonstrated that the optimum conditions for immobilization were as follows: the range of optimum concentration of solution papain was 1.0-(2.0 mg/mL),pH value was 7.0 and the time for immobilization was 2 h. The maximal activity of the immobility papain was 111.1 U/g and the activity recovery of the immobility papain was 57.9%.
     试验结果表明,当溶液酶质量浓度为1.0~2.0 mg/mL、pH 7.0、固定2 h时,固定化酶活力最高达111.1 U/g,活力回收达57.9%.
短句来源
     The β-glucanase from strain GXC of Trichoderma reesei was purified in three steps which comprised ammonium sulfate precipitation, Sephadex G-100 chromatography, and DEAE-Sephadex A-50 chromatography. The purified enzyme showed an activity increase of 14.60 fold, and an activity recovery of 6.62%.
     对里氏木霉所产β-葡聚糖酶粗酶液通过饱和硫酸铵沉淀、Sephadex G-100 柱层析和DEAE-Sephadex A-50 柱层析进行纯化,比活提高14.60倍,活力回收6.62%。
短句来源
     the temperature was 4 ℃ ; the immobilizing time was 6 h; and the pH value was 7.5. The activity and activity recovery of the immobilized papain were 1 786.93 U/g and 69.54% , respectively.
     研究结果表明,最佳的固定化条件为:给酶量0.36mg/g(蛋白质质量浓度为0.12 mg/mL)、pH 7.5、温度4℃左右条件下,固定6 h,所得到的固定化酶活力为1 786.93 U/g,活力回收高达69.54%.
短句来源
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  活力回收率
     The results were as follows: the optimum load of enzyme was 50mg/100mL,chitosan was 0.2%, at 50℃ and pH=7 5. The activity recovery of the immobilization of papain was 69.8%.
     结果表明:木瓜蛋白酶的最佳固定化条件为:给酶量为50mg/100mL、壳聚糖浓度为0.2%、pH=7.5、50℃温度下,所得固定化木瓜蛋白酶活力回收率可达69.8%。
短句来源
     The results were as follows: the optimum load of enzyme was 40~50mg/g carrier, crosslinking for 12h with 0.4%~0.5%glutaraldehyde at 25~30℃and pH7.5. The activity recovery of the immobilizated papain was 61.6%respectively.
     结果表明:木瓜蛋白酶的最佳固定化条件为给酶量为40~50mg/g,于pH7.5,25~30℃下,0.4%~0.5%的戊二醛溶液交联12h,所得的固定化木瓜蛋白酶的活力回收率平均达61.6%。
短句来源
     When the concentration of gelatin was 150 g/L, the concentration of glutaraldehyde was 0.5%, the lactase amount was 5 g/L, pH value was 7.2 and mixing round time was 3 minutes, the result of lactase activity recovery ratio was up to 78.12%.
     当明胶质量浓度为150g/L,交联剂戊二醛的体积分数为0.5%,酶添加量为5g/L,在pH值为7.2,搅拌时间3 min的条件下制备固定化乳糖酶,其酶活力回收率可达78.12%。
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
     The activity,the activity recovery ratio and the activity express ratio of BFIGI Ⅱ were 811.39 U/g,53.67% and 72.97% respectively.
     每克固定化酶Ⅱ的总活力为 811 39U ,活力回收率为 5 3 6 7% ,活力表现率为 72 97%。
短句来源
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  活性回收率
     The purity ,specific activity,recovery rate of activity,relative molecular weight (M.W)and PI were over 98%,2.4×10 7IU/mg, 14%,19800 and 5.0 respectively .
     纯化的rhIFN α1b的纯度为 98%以上 ,比活性 2 .4× 10 7IU/mg ,活性回收率 14 % ,相对分子质量 1980 0和等电点 5 .0。
短句来源
     Results Through dye affinity chromatography column immobilized with Cibacron Blue F3GA,EDH purification factor was 2.0,activity recovery was 30.8%;
     结果经过固定有Cibacron Blue F3GA的亲和层析柱,乙醇脱氢酶的纯化倍数为2.0,酶活性回收率为30.8%;
短句来源
     and through dye affinity chromatography column immobilized with Red KE-3B,G-6-PDH purification factor was 23.2,activity recovery was 66.0%.
     经过固定有KE-3B艳红的亲和层析柱,葡萄糖-6-磷酸脱氢酶的纯化倍数为23.2,酶活性回收率为66.0%。
短句来源
     The protein mass yield of rhIFNα-2b under the optimum condition was 4.2 times higher than that of dialysis refolding process. The activity recovery rate was 68.7% with the specific activity of 1.77×108IU/mg,and purity of 90%.
     结果表明,复性后rhIFNα-2b的蛋白收率是透析复性法的4.2倍,活性回收率为68.7%,比活力1.77×108IU/mg,纯度高于90%。
短句来源
     The total activity recovery of this purification method was 52.6% and the purification factor was 3.87.The final specific activity of recombinant NbAChE was 2837(U/mg).
     该方法的活性回收率为52.6%,纯化因子为3.87; 纯化后AC hE的比活为2 837U/m g。
短句来源
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  活回收率
     The results demonstrated the activity recovery of the three immobilized tripsin were 81.9%,80.1%,(44.8%).
     研究表明,三种载体固定胰蛋白酶时的酶活回收率依次为81.9%、80.1%、44.8%。
短句来源
     The activity recovery of immobilized GST reached 41.6%, optimal pH 6.5~7.0, optimal temperature 37℃ and the thermal stability of immobilized GST wasenhanced.
     结果固定化酶活回收率可达41.6%,最适pH6.5~7.0,最适温度37℃,对底物(CDNB和GSH)的亲和力略有下降,对温度稳定性大大提高。
短句来源
     The studies on the immobilization of tannase indicated that when 0.1g chitosan reacted with 3% glutaraldehyde 5 ml for 4 h, then reacted with 58.4 u tannase for 4 h at 4 °C , the activity recovery of tannase was 73%.
     比较几种固定化载体 ,确定以壳聚糖为载体 ,用戊二醛作交联剂制得固定化单宁酶。 壳聚糖用量 0 .1g,用 3%戊二醛 5 ml交联 4 h,然后加入酶 5 8.4 u,于 4°C反应 4 h,固定化酶活回收率可达 73%。
短句来源
     Results:The activity recovery of immobilized GST reached 41.6%,optimal pH 6.5~7.0,optimal temperature 37℃ and the thermal stability of immobilized GST was enhanced.
     结果 :固定化酶活回收率可达 4 1.6 % ,最适pH6 .5~ 7.0 ,最适温度 37℃ ,对底物 (CDNB和GSH)的亲和力略有下降 ,对温度稳定性大大提高。
短句来源
     Our results showed that the maximum 0 52 U/cm 2 activity of immobilized lipase and 20% activity recovery were obtained by NaIO 4 method.
     结果表明,在适宜条件下,高碘酸钠氧化法获得的固定化酶活最高,达052U/cm2,酶活回收率为20%。
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  activity recovery
Addition of the same concentration of polysorbate 80 to the reconstitution medium caused an increase in activity recovery for each formulation, but the overall pattern remained unchanged.
      
Annealing of sucrose-glycine formulations causes a small but significant decrease in activity recovery relative to unannealed controls, whereas no annealing effect is observed with sucrose-only formulations.
      
In a sucrose-only excipient system, activity recovery of both model proteins is about 80% and is independent of sucrose concentration over a range from 1 to 40 mg/mL.
      
However, the high activity recovery in the presence of detergents, as the stripping agent, suggests that they can constitute suitable replacement for the more expensive and common stripping agent of cyclodextrins.
      
These findings may assist the activity recovery of recombinant proteins at relatively high concentrations.
      
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