Using Rice Flour for Purification of Maltose Binding Fusion Proteins Expressed in Escherichia coli Azadeh Neissi, Masoudreza Seyfi Abad Shapouri, Masoud Ghorbanpoor
Author(s):
Abstract:
Background
One disadvantage of expressing heterologous proteins in Escherichia coli is that the proteins are frequently expressed as insoluble inclusion bodies. To avoid this problem, heterologous proteins are typically expressed as a fusion protein. Maltose binding protein (MBP) is one of the widely used partners for production of recombinant fusion proteins in E. coli. MBP is among the most effective solubility enhancers. In addition, MBP can be used as an affinity tag for purification of recombinant proteins on a column of amylose resin. Objectives
The purpose of this study was to investigate the use of rice flour, a natural source of amylose, for purification of MBP fusion proteins. Materials And Methods
MBP and a fusion protein of MBP and avian influenza virus nucleoprotein (MBP-NP) were expressed in E. coli and subjected to purification by rice flour and a commercial amylose resin. The purified proteins were analyzed by SDS-PAGE. Results
The results indicated that MBP and MBP NP, both were successfully purified by rice flour. Conclusions
Rice flour can be used for purification of MBP fusion proteins. Although the efficiency of purification by rice flour is less than amylose resin, however, the yield is sufficient to obtain a quantity of protein required for research purposes.Keywords:
Maltose , Binding Proteins , Fusion , Protein , Amylose , Purification , Rice , Flour
Language:
English
Published:
Jundishapur Journal of Microbiology, Volume:6 Issue: 3, May 2013
Page:
127
https://magiran.com/p1137555
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