渗透休克法提取重组青霉素G酰化酶及酶学性质研究

Properties of Recombinant Penicillin G Acylase Extracted from Escherichia coli by Osmotic Shock

为简化后期提取工艺,采用渗透休克法提取基因工程菌重组青霉素G酰化酶,回收率92.4%的酶蛋白释放到胞外,纯度达80%,比酶活26.4 U/m g.酶学性质研究表明,K cPGA的最适作用pH和温度分别为pH 7~9和50℃,在pH 5.0~8.0和低于40℃的范围较稳定.

To simplify the purification process,an extract method of osmotic-shock was used to seperate penicillin G acylase from E.coli.92.4% of PGA was released to the buffer solution,the purity and specific enzyme activity reached 80% and 26.4 U/mg,respectively.The optimum reaction temperature and pH of KcPGA were 50 ℃ and pH 7～9,and it was stable at 40 ℃ and pH 5.0～8.0.