Cloning and expression of a tomato glutathione S- transferase (GST) in Escherichia coli

chromatography and biochemically characterized. The results show that the optimal conditions for the expression of recombinant ShGSTU1 in E. coli were growth under 37°C, and 4-h IPTG induction with 1 mM concentration. About 18.93 mg ShGSTU1 was recovered from 1 g wet bacteria. The recombinant ShGSTU1 exhibited enzymatic activity with specific activity 0.625 U/mg. These results might provide a significant foundation for the later research on the mechanism of ShGSTU1 in tomato resistance to powdery mildew.