Galactose induces the expression of penicillin acylase under control of the lac promoter in recombinant Escherichia coli
Galactose induces the expression of penicillin acylase under control of the lac promoter in recombinant Escherichia coli
复制标题
半乳糖在重组大肠杆菌中诱导 lac 启动子控制下青霉素酰化酶的表达
作者：
A. De león;Graciela B. Breceda;A. P. Barba de la Rosa;J. F. Jiménez;Rubén López
以半乳糖为诱导剂，将青霉素酰化酶(PA)克隆到野生型lac启动子控制的pPA102载体中，在大肠杆菌JM101、JM103和JM105转化细胞中进行表达。大肠埃希菌JM101/pPA102的PA比活力最高。对于以大肠杆菌JM101/pPA102为基础的大规模PA生产，以半乳糖代替异丙基硫代半乳糖苷作为诱导剂也同样成功，而且成本更低。
The expression of penicillin acylase (PA), cloned in the pPA102 plasmid under control of the wild-type lac promoter and using galactose as inducer in Escherichia coli JM101, JM103 and JM105 transformant cells, was analyzed. The E. coli JM101/pPA102 cultures attained the highest specific activity of PA. For large scale PA production based on E. coli JM101/pPA102 a culture media with galactose instead of isopropyl-thio-galactopyranoside as inducer would be as successful and less expensive.