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| Fusing the Acyl Carrier Protein Enhances the Solubility and Thermostability of the Recombinant Proteins in Escherichia coli |
| LIU Yan-juan1, LI Xu-juan2, YUAN Hang1, LIU Xian1, GAO Yan-xiu1, GONG Ming1, ZOU Zhu-rong1 |
1. Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, School of Life Sciences, Yunnan Normal University, Kunming 650500, China;
2. Sugarcane Research Institute, Yunnan Academy of Agricultural Sciences, Kaiyuan 661600, China |
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Abstract At present, protein solubility and thermostability has become an unavoidable problem for the efficient production, functional application and long-term preservation of the recombinant proteins. Regarding this, the strategy by using acidic protein fusion tags appears to be an effectual solution. Acyl carrier protein (ACP), an essential component of fatty acid biosynthesis pathway, is a small and highly acidic peptide in Escherichia coli. It was in-frame fused with several heat-labile target proteins[e.g. the ascorbate peroxidase 1 of Jatropha curcas (JcAPX1), the activase isoform 2 of ribulose-1,5-bisphosphate carboxylase/oxygenase of soybean (GmRCA2), the homoserine O-transsuccinylase of E. coli (EcMetA)] at the gene level for inducible expression in E. coli. ACP fusion could significantly enhance the solubility and thermostability of all these recombinant target proteins, and also effectively protect enzyme JcAPX1 from heat inactivation, with increased heat tolerance of at least 2℃. Presumably, this effect of ACP might be related to its high acidity, and it could be used as a novel functional acidic fusion tag in future studies.
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Received: 09 January 2017
Published: 25 July 2017
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