Expression and Purification of the Vespa basalis venom-Mastoparan B peptide in Escherichia coli

碩士 === 國立虎尾科技大學 === 光電與材料科技研究所 === 97 === 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 s...

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Bibliographic Details
Main Authors: Jia-Yang Hong, 洪嘉陽
Other Authors: Chi-Chung Peng
Format: Others
Language:zh-TW
Published: 2009
Online Access:http://ndltd.ncl.edu.tw/handle/3n97df
Description
Summary:碩士 === 國立虎尾科技大學 === 光電與材料科技研究所 === 97 === 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.