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活力回收
    The condition of immobilization was experimented too and a good result was achieved: when the chitosan particle was treated with 3 % solution of glutaraldehyde at 4 -6℃ for 6 h and then was incubated in solution of papain(pH7. 2,2.5 mg/ml) for 15 hthe immoblized papain was prepared with activity recovery of 50 % .
    以微晶壳聚糖为载体,戊二醛为交联剂将木瓜蛋白酶固定化。 3%戊二醛在4℃~6℃下处理微晶壳聚糖6h,加酶液固定15h,活力回收达50%。
    Three crosslinking agents (glutaraldehyde, chloroacetic acid and epichlorohydrin) were respectively used to immobilize AS 1 398 neutral proteinase. The activity recovery of immobilized enzyme reached 77% when glutaraldehyde 0 3%, pH8 0, treating time of chitosan 8~10h, enzymatic liquid 15ml(40mg/ml protein), immobilized time 8h. The optimum temperature and optimun pH of immobilized enzyme was 55℃ and8 0 respectively.
    确定 0 .3%戊二醛在 30℃ ,p H8.0的条件下处理壳聚糖 8~ 1 0 h,加酶液 ,固定 8h,酶活力回收约为 77% ,固定化酶最适作用温度为 55℃ ,最适作用 p H为 8.0 ;
    The activity recovery of immobilized enzyme is around 50% and relative enzyme activity 74% under these conditions. MIE can clarify beer and prevent cold turbid.
    此条件下制得的磁性酶活力回收在 5 0 %左右 ,相对酶活力达 74 % ,该磁性酶对啤酒澄清防止冷浑浊有明显效果
    After sonication of the pellets,the supernatant was treated by 55℃ for 15min as the first step of this method. Subsequently,ammonium sulfate fractionation and Q Sepharose fast flow,Pheny1 Sepharose fast flow Superose 12 column chromatography were performed to purify hydantoinase from Pseudomonas 2262 to reach SDS PAGE pure. The analysis of enzymatic activity shown that the activity recovery was 15.6%,specific activity was 18.37U/mg and the purification factor was 59.3 respectively.
    菌体经超声波处理后 ,上清液首先用热变性作为纯化的第一步 ,后经硫酸铵沉淀和 Q- Sepharose fast flow阴离子交换柱 ,Phenyl- Sepharose fast flow疏水层析 ,Superose12凝胶排阻层析等步骤 ,从 Pseudomonas2 2 6 2菌体中获得电泳纯的海因酶 ,酶活力回收 15 .6 % ,比活为 18.37U/ m g,提纯倍数为 5 9.3。
    In the re-utilization experiments the activity of immobilized trypsin reached 5907.20 U·g -1 .CONCLUSION The activity units and activity recovery prepared immobilized trypsin were high, which is good for its application to industry.
    回收再利用实验得到的固定化胰蛋白酶活力单位仍高达 5 90 7.2 0U·g-1 。 结论 制备的固定化胰蛋白酶活力单位高 ,活力回收也较高 ,有利于工业运用
    After solidification in the solution for 45 min followed by filtration,rinsing and drying,immobilized enzyme beads were gained with a 34.1% activity recovery of the total enzyme added.
    固定化酶的活力回收约为34.1%.
 

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