Abstract—Mastoparan B (MPB), a cationic venom peptide found in Vespa basalis, belongs to an evolutionarily conserved component of the innate immune response against microbes. MPB possesses significant biological potency, especially in the anti-microbial activity, and pore-forming ability. These properties make MPB extremely attractive for further studies and applications. However, this cationic MPB is difficult to obtain and production. In the present study, we successfully to develop a new and reliable recombinant oleosin-based fusion expression procedure in Escherichia coli and coupled with the artificial oil bodies (AOB)-cyanogen bromide purification platform to produce bioactive MPB. This procedure could yield ~2.0mg of MPB from 1L of cultured cell pellet. And, enhanced the yield by >2-fold of purified MPB compared to reported previously. Take together, this study provides a new insight into the over-production of active MPB, which will facilitate studies and applications of this peptide in the future.

 

Index Terms—artificial oil bodies, cyanogen bromide, Escherichia coli, mastoparan B, oleosin-fusion protein

Cite: Feng-Chia Hsieh and Tzyy-Rong Jinn, "Efficient Production of Mastoparan B, a Cationic Venom Peptide, via the Artificial Oil Body-Cyanogen Bromide Purification Platform," International Journal of Food Engineering, Vol. 2, No. 2, pp. 151-154, December 2016. doi: 10.18178/ijfe.2.2.151-154