Recombinant bacterial expression of the lysozyme from the tobacco-hornworm Manduca sexta with activity at low temperatures.
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Garcia-Orozco KD, Lopez-Zavala AA, Puentes-Camacho D, Calderon-de-la-Barca AM, Sotelo-Mundo RR
Recombinant bacterial expression of the lysozyme from the tobacco-hornworm Manduca sexta with activity at low temperatures.
Biotechnol Lett. 2005 Aug;27(15):1075-80.
- PubMed ID
- 16132856 [ View in PubMed]
- 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.