Abstract—Mastoparan B is a cationic, amphiphilic tetradecapeptide toxin isolated from the venom of the black-bellied hornet (Vespa basalis), the most dangerous species of wasps found in Taiwan. Mastoparan B was evaluate possess antibacterial activity and cardiovascular depress activity. However, mastoparan B is low abundance in the venom (3.4% of crude venom). In this study, mastoparan B was overexpressed in Escherichia coli BL21 as a recombinant protein fused the C-terminus of oleosin by a linker polypeptide, intein S. Artifical oil bodies (AOBs) were reconstituted with triacylglycerol, phospholipid to obtain the insoluble recombinant protein. Mastoparan B was subsequently released through self-splicing of intein induced by temperature alteration from artifical oli bodies, and the recombinant mastoparan B was collected it in the supernatant after centrifugation. Recombinant mastoparan B release from AOBs was exhibited membrane permeabilization activity, bacteriostatic and bactericidal activity. These results have shown that mastoparan B was successfully expressed and purified via the efficient AOB expression/purification system.

Index Terms—Vespa basalis, mastoparan B, artifical oil bodies (AOBs) expression/puruification system, bacteriostatic and bactericidal activity.

C. C. Peng is with the Department of Biotechnology, National Formosa University, Taiwan
J. Y. Hong is with the Graduate Institute of Electro-Optical and Materials Science, National Formosa University, Taiwan
W. C. Tu is with the Department of Entomology, National Chung-Hsing University, Taiwan (e- mail: bocky@sunws.nfu.edu.tw).

Cite: Chi-Cung Peng, Jia-Yang Hong, and Wu-Chun Tu, "Cost-Effective Expression and Purification of Recombinant Venom Peptide Mastoparan B of Vespa Basalis in Escherichia Coli," International Journal of Bioscience, Biochemistry and Bioinformatics vol. 2, no. 5, pp. 309-313, 2012.