ArticleTurkish journal of biology = Turk biyoloji dergisi2018
Cloning and soluble expression of mature α-luffin from Luffa cylindrica in E. coli using SUMO fusion protein.
Article in Turkish journal of biology = Turk biyoloji dergisi, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- Production of an Antibody Fragment (scFv) Targeting PcrV Protein of Pseudomonas aeruginosa in Fed-Batch Cultivation ModeIranian biomedical journal · 2021Article
- Maltose Induced Expression of Cecropin AD by SUMO Technology in Bacillus subtilis WB800N.The protein journal · 2020Article
- Molecular cloning and in-depth bioinformatics analysis of type II ribosome-inactivating protein isolated fromSaudi journal of biological sciences · 2020Article
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6 authors.
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Abstract
α-Lufin, found in Luaf cylindrica seeds, is a type I ribosome inactivating proteins. Cytotoxic effects make it an appropriate candidate for the construction of immunotoxins and conjugates. Because of limited natural resources, recombinant technology is the best approach to achieve large-scale production of plant-based proteins. In the present study, α-lufin protein was expressed in E. coli and the effects of different temperature conditions, SUMO fusion tag, and cultivation strategies on total expression and solubility were investigated. Protein expression was evaluated at different intervals (0, 4, 6, 8, 24 h) postinduction. Our results showed that EnBase had higher eficiency 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.
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