高温乳糖酶基因在大肠杆菌中的高效表达

High-level expression of thermostable galactosidase gene in Escherichia coli

来源于嗜热脂肪芽孢杆菌 (Bacillusstearothermophilus)的 β -半乳糖苷酶基因bgaB经克隆、测序后 ,转入大肠杆菌高效表达载体pET - 2 0 (b)中。重组菌在IPTG诱导下 ,表达出的重组蛋白比酶活量为 6 6 6U/mg ,比出发菌株高 5 0倍。

The bgaB gene from Bacillus stearothermophilus encoding a thermostable beta-galactosidase was cloned and sequenced and then expressed into E.coli T7 expression system.using pET-20(b). The expression level reached 6.66U/mg protein after IPTG inducing, which is 50 times higher than that of original strain.