Cloning and soluble expression of mature α-luffin from Luffa cylindrica in E. coli using SUMO fusion protein

Abstract

α-Luffin, found in Luffa cylindrica seeds, is a type I ribosome inactivating proteins. Cytotoxic effects make it an appropriatecandidate for the construction of immunotoxins and conjugates. Because of limited natural resources, recombinant technology is thebest approach to achieve large-scale production of plant-based proteins. In the present study, α-luffin protein was expressed in E. coliand the effects of different temperature conditions, SUMO fusion tag, and cultivation strategies on total expression and solubility wereinvestigated. Protein expression was evaluated at different intervals (0, 4, 6, 8, 24 h) postinduction. Our results showed that EnBase hadhigher efficiency than LB, and maximum solubility and total protein expression were achieved 24 h after induction at 30 °C and 25 °C,respectively. It was shown that SUMO tag is an effective strategy to improve protein solubility.