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  • Title: Recombinant bacterial expression of the lysozyme from the tobacco-hornworm Manduca sexta with activity at low temperatures.
    Author: García-Orozco KD, López-Zavala AA, Puentes-Camacho D, Calderón-de-la-Barca AM, Sotelo-Mundo RR.
    Journal: Biotechnol Lett; 2005 Aug; 27(15):1075-80. PubMed ID: 16132856.
    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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