Abstract
Self-assembling amphipathic peptides (SAPs) are a category of peptides that have unique sequences with alternating hydrophobic and hydrophilic residues that can spontaneously assemble into ordered nanostructures. In this study, we investigated the potential of fusion technique with SAPs to improve the thermal stability of lipoxygenase (LOX) from Pseudomonas aeruginosa. Six SAPs were individually fused to the N terminus of the LOX that resulted to the SAP–LOX fusions with approximately 2.3- to 4.5-fold enhanced thermal stability at 50 °C. The specific activities of the SAP–LOX fusions were also increased by 1.0- to 2.8-fold as compared with the wild-type LOX. This is the first report on the improvement of the thermal stability and specific activity of an enzyme by the fused SAPs, suggesting a simple technique to improve the catalytic properties of the recombinant enzymes by fusion expression.
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Acknowledgments
We would like to thank Professor Byong H. Lee for critical reading and suggestions on the manuscript. This work was supported by the National Natural Science Foundation of China (no. 31171639, no. 31000031, and no. 31070711), the National High Technology Research and Development Program of China (No. 2011AA100905), the NCET-10-0461, the Natural Science Foundation of Jiangsu Province (No. BK2010147), and the Independent Innovation Program of Jiangnan University (JUSRP11215).
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Lu, X., Liu, S., Zhang, D. et al. Enhanced thermal stability and specific activity of Pseudomonas aeruginosa lipoxygenase by fusing with self-assembling amphipathic peptides. Appl Microbiol Biotechnol 97, 9419–9427 (2013). https://doi.org/10.1007/s00253-013-4751-y
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DOI: https://doi.org/10.1007/s00253-013-4751-y