利用大腸桿菌表達與純化黑腹胡蜂蜂毒胜肽-Mastoparan B

Mastoparan B has antibacterial activity and hypotension activity isolated from the venom of the hornet Vespa basalis. However, Mastoparan B is few in the venom. In this study, Mastoparan B purified via Artifical oil bodies (AOBs) expression/puruification system. At first Mastoparan B was overexpressed in Escherichia coli BL21 as a recombinant protein fused the C-terminus of oleosin by a linker polypeptide, intein S. AOBs were reconstituted with triacylglycerol, phospholipid to obtain the insoluble recombinant protein. Mastoparan B was subsequently released through self-splicing of intein S induced by temperature and pH alteration from artifical oli bodies, and the recombinant Mastoparan B was collected it in the supernatant after centrifugation. The results have shown the purified Mastoparan B exhibited bacteriostatic and bactericidal activity for Strep- tococcus alactolyticus, Staphylococcus aureus, Salmonella Cholerasuis Staphy- lococcus intermedius B and Vibrio Parahaemolyticus but for Staphylococcus xy- losus had only bacteriostatic activity.