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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%。
    After the three-step treatment, purification fold is 6.7 with 67.14% enzyme activity recovery and single band shows by PAGE determination.
    纯化倍数达到6.7,酶活回收率为67.14%。
    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。
    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%。
    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%。
    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。
    In such conditions the activity recovery of the immobilized alcalase reached 63.8%.
    在此条件下得到的固定化碱性蛋白酶活回收率可达63.8%。
    After a two-step treatment, ten-fold purification was obtained with 24% enzyme activity recovery.
    经过Q-sephrose FF离子交换层析,得到分子量为22.0 KDa电泳纯的木聚糖酶,其酶活回收率为24%,纯化倍数10倍。
    During fluid bed drying, the activity recovery of all the enzymes investigated was more than 90%. The optimal inlet temperature was chosen as 40 ℃.
    在制备过程中进风温度为 4 0℃ ,酶活回收率达到 90 %以上 .
    In this article, the Glucoamylase was immobilized onto the polyvinyl alcohol complex gel The results showed that the activity of immobilized Glucoamylase was 1,558 U per gram dry gel,the activity recovery was 30 2% The enzyme system could directly converted 10% starch hydrolyses to glucose under the conditions of pH4 6 and 45℃ The results showed that the working half life of immobilized Glucoamylase was 350 hours The immobilized Glucoamylase has excellent store and working stability
    以聚乙烯醇复合凝胶作为载体固定化糖化酶 ,最终酶活达到 1,5 5 8u/ g干胶 ,酶活回收率是 30 2 %。 该固定化酶在 pH4 6 ,4 5℃下 ,以 10 %的可溶性淀粉为底物进行分批试验 ,操作半衰期为 35 0h ,具备高底物浓度下操作及贮存稳定性
    The result showed that the optimal temperature of immobilized Glucoamylase was 55 ℃~58 ℃ and optimal pH-value was 5.0.However the storage and operation stability were better than free enzyme, and after 8 months the activity kept about 94% and it had been used 43 batches time after time. The activity recovery of immobilized Glucoamylase was 56%.
    结果表明 ,该固定化酶最适 p H值为 5. 0 ,最适温度为 55~ 58℃ ,而且具有较好的贮存稳定性和操作稳定性 , 8个月后该固定化酶的残余活力仍保持在 94%左右 ,可重复使用 43批次 ,此固定化酶酶活回收率达到 56% .
    The activity recovery of industrial lipase with the mixed reverse micelles formed from CTAB with TRPO was about 70%, which was the best in these mixed reverse micelles tested.
    通过测定反萃水相的酶活,发现CTAB? TRPO混合反胶团的效果最好,酶活回收率最高,可以达到70%.
    98.98% of degree of immobilization can be achieved when the adsorption procedure was performed in the presence of heptane. The hydrolytic activity and the apparent activity recovery of lipase adsorbed on resin in heptane was 4.07 and 3.43 times higher than that of lipase adsorbed in sodium phosphate buffer, respectively.
    分别以正庚烷及磷酸盐缓冲液作为固定化介质,发现在正庚烷介质中树脂NKA的固定化效率能够达到98.98%,与采用磷酸盐缓冲液作为介质相比,固定化酶的水解活力和表观酶活回收率分别提高了4.07和3.43倍。
    Conclusions: β-1,3-Glucanase of electrophoresis grade was obtained by ammonium sulfate two-step salting-out and anion-exchange chromatography,and its activity recovery was high.
    结论:采用硫酸铵分段盐析和离子交换层析法可获得电泳纯的β-1,3-葡聚糖酶,且酶活回收率高。
    Under the optimal conditions,the activity recovery of immobilized pectinase can reach to more than 80%.
    在此条件下固定化果胶酶的酶活回收率达到80%以上。
 

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