The mutant was overexpressed in Escherichia coli BL21(DE3) by IPTG induction.
IPTG诱导突变体在大肠杆菌BL21（DE3）中高效表达。
The modified gene was expressed by IPTG induction and purified by affinity chromatography and cleavage in place.
IPTG诱导该基因的表达，亲和层析和原位裂解法纯化表达产物。
The induction temperature, induction time, and IPTG concentration were also optimized by a series of experiments. Further purification modes of this protein were also explored.
同时还进行梯度实验分别对诱导的温度、时间和IPTG诱导时菌体浓度进行优化，并对蛋白的纯化方案进行摸索。
The recombinant plasmids containing mutant genes were transformed into the Escherichia coli strain BL21 (DE3), and the expressed proteins were found to be water soluble after the induction of IPTG.
将含突变基因的重组质粒转化大肠杆菌菌株bl2 1 (DE3)，经IPTG诱导表达获得的目的蛋白质均以可溶形式存在。
The recombinant plasmids containing mutant genes were transformed into the Escherichia coli strain BL21 (DE3), and the expressed proteins were found to be water soluble after the induction of IPTG.
将含突变基因的重组质粒转化大肠杆菌菌株bl2 1 (DE3)，经IPTG诱导表达获得的目的蛋白质均以可溶形式存在。
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