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活力回收率
    After lyophilization and Sephadex G-25 chromatography, the mating pheromone activity showed an increase of 3 fold and an activity recovery of 24%.
    经冷冻干燥和Sephadex G-25柱层析,样品中交配信息素的活力提高到了3倍,活力回收率24%。
    The experiment results show that DAS are coupled with theamino supports loading 1.0~2.0mmol/g of –NH2 firstly(aldehyde:amino(mole)=5),then papain are coupled with the flexible support, and activity recovery ofimmobilized papain is 40~50% on the flexible support, whereas only 20~30% on armspacer support.
    结果表明:先将 DAS 柔性链偶联于胺基担载量在 1.0~2.0mmol /g 的胺基载体上,控制DAS 的醛基适度过量于胺基,所得到的柔性载体对酶固定化,其酶活力回收率可达 40~50%,比手臂固定化酶高出 2~3 倍;
    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%;
    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%。
    At 32℃ and 0.15Mpa, the ultrafiltrating ratio is 90%, the SOD activity recovery could reach 88.1%, specific activity of SOD and enzyme activity were 21.1U/mg and 22.11U/ml, respectively.
    在此条件下,酶活力回收率最大可达88.1%,比活力和单位酶活力分别为21.1U/mg和22.11U/ml。
    Under optimum conditions for the coupling, the apparent activity and activity recovery of immobllized pectinase were 1980u/g and 87 % respectively.
    在以上最适条件下,固定化果胶酶的表观活力为1980U/g,活力回收率为87%。
    When the amount of lipase is between 168u/g silk to 308u/g silk,the activity of immobilized lipase is between 106u/g silk to 160u/g silk and the activity recovery is quite high (above 52%).
    加酶量为168~308u/g蚕丝时,所得固定化脂肪酶活力为106~160u/g蚕丝,此时固定化酶的活力回收率较高(>52%)。
    The optimum conditions for immobilization were as follows: Chitosan was treated with 5% solution of qlutaraldehyde at 30℃ for 8h, then 10ml solution of trypsin (0.3mg/ml pH7. 0 ) was inunobilized on the carrier. Enzyme activity recovery was 67 %~75%.
    5%戊二醛在30℃下处理载体8h,加10ml酶液(0.3mg/ml,pH7.0)固定12h以上,活力回收率达67%-75%。
    When the amount of lipase is 400u/(g CADB)~1200u/(g CADB),the activity of immobilized lipase is 193u/(g CADB)~448u/(g CADB)and the activity recovery is above 37%.
    加酶量为 40 0 u/g~ 1 2 0 0 u/g(载体 )时 ,所得固定化酶活力为 1 93u/g~ 448u/g(载体 ) ,此时固定化酶的活力回收率较高 (>37% )。
    The activity recovery of immobilized cells was over 70%.
    试验结果表明 :固定化后细胞的活力回收率≥ 70 % ;
    The results were as follows: the optimum load of enzyme was 1.92 mg enzyme/g carrier, the absorbing time was 12 h and the temperature 4~8 ℃; then interacted for 3 h at 4~8 ℃ with 0.5% glutaraldehyde. The activity and the activity recovery of the immobilized papain were 38.49 U/g carrier and 66.60% respectively.
    结果显示 :木瓜蛋白酶的最佳固定化条件是给酶量为 1 .92mg/g、4~ 8℃吸附 1 2h、再用体积分数为 0 .5 %的戊二醛溶液于 4~ 8℃交联 3h ,所制得的固定化木瓜蛋白酶活力达 38.49U/g ,酶活力回收率平均达 6 6 .6 0 % ,高于同类研究水平
    In order to investigate the recognition mechanism and the relationship between structure and function of tRNA Trp with tryptophanyl tRNA synthetase (TrpRS), TrpRS from Bacillus subtilis was purified and immobilized on CNBr activated Sepharose 4B. Protein recovery and activity recovery of the immobilization were 95.5% and 31.3%, respectively. Properties of immobilized TrpRS were studied in detail.
    为研究tRNATrp 与色氨酰tRNA合成酶(TrpRS) 的相互识别及其结构、功能关系, 纯化了枯草杆菌TrpRS并用溴化氰活化的Sepharose 4B 将TrpRS固定化, 固定化TrpRS的蛋白质回收率为95 .5 % , 活力回收率为31.3% 。
    In order to investigate the recognition mechanism and the relationship between structure and function of tRNA Trp with TrpRS,TrpRS from Bacillus Subtilis was purified and immobilized on CNBr\|activated Sepharose 4B.Protein recovery and activity recovery of the immobilization were 95 5% and 31 3%,respectively. Properties of immobilized TrpRS were studied in detail.
    为研究 t RNATrp与色氨酰 - t RNA合成酶 ( Trp RS)的相互识别及其结构与功能的关系 ,纯化了枯草杆菌 Trp RS,并用溴化氰活化的 Sepharose4B将 Trp RS固定化 ,固定化 Trp RS的蛋白回收率为 95.5% ,活力回收率为 31 .3% .
    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%。
    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%。
    The results showed that the specific activity of the purified bromelain was 937 u/mg protein with activity recovery of 48% and the purification multiple was 8.0.
    以陶瓷柱层析结合超滤法纯化果菠萝蛋白酶 ,产品比活力 937u/ mg蛋白 ,活力回收率 48% ,纯化倍数 8
    The activity, the activity recovery ratio and the activity express ratio of FPIA were 509.09 U/g, 58.33% and 83.454% respectively.
    每克粉末状丝素固定化酶的总活力为 5 0 9.0 9U,活力回收率为 5 8.33% ,活力表现率为 83.4 5 % .
    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%。
    The activity,the activity recovery ratio and the activity express ratio of FPIGI were 844 U/g,55.27% and 72.42% respectively.
    每克固定化酶Ⅲ的总活力为 84 4U ,活力回收率为 5 5 2 7% ,活力表现率为 72 4 2 %。
    The agglutinating activity of the purified lectin (BOL) increased 32 times and the activity recovery is 75 %.
    BOL的比活性比粗提液提高了 32倍 ,活力回收率达 75 % .
 

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