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Recombinant Bacterial Expression of the Lysozyme from the Tobacco-Hornworm Manduca sexta with Activity at Low Temperatures

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Abstract

A gene coding for lysozyme from the insect Manduca sexta (Ms-lyz) was expressed in Escherichia coli. The protein was produced as an insoluble cytoplasmic inclusion body which was denatured in 8 M guanidine-HCl, renatured and purified by affinity and ion-exchange chromatography. The N-terminal sequence and the activity of the recombinant protein against Micrococcus luteus confirmed that correct expression had occurred. When Ms-lyz activity was compared to hen egg white lysozyme, the insect lysozyme was active at lower temperatures. These results demonstrate the feasibility of producing a disulfide-bonded lysozyme enzyme in bacteria and suggest that the insect Ms-lyz is an interesting system for further development of an antibacterial functional at low temperatures.

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Correspondence to Rogerio R. Sotelo-Mundo.

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García-Orozco, K.D., López-Zavala, A.A., Puentes-Camacho, D. et al. Recombinant Bacterial Expression of the Lysozyme from the Tobacco-Hornworm Manduca sexta with Activity at Low Temperatures. Biotechnol Lett 27, 1075–1080 (2005). https://doi.org/10.1007/s10529-005-8452-1

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  • DOI: https://doi.org/10.1007/s10529-005-8452-1

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