Enhancing the Solubility of Recombinant Proteins in Escherichia coli by Using Hexahistidine-Tagged Maltose-Binding Protein as a Fusion Partner

2010 ◽  
pp. 259-274 ◽  
Author(s):  
Ping Sun ◽  
Joseph E. Tropea ◽  
David S. Waugh
Keyword(s):  
Escherichia Coli ◽  
Recombinant Proteins ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Fusion Partner

Extracellular production and affinity purification of recombinant proteins with Escherichia coli using the versatility of the maltose binding protein

2009 ◽  
Vol 140 (3-4) ◽  
pp. 194-202 ◽  
Author(s):  
Benjamin Sommer ◽  
Karl Friehs ◽  
Erwin Flaschel ◽  
Michael Reck ◽  
Frank Stahl ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Recombinant Proteins ◽  
Binding Protein ◽  
Affinity Purification ◽  
Maltose Binding Protein ◽  
Extracellular Production

scholarly journals The remarkable solubility-enhancing power of Escherichia coli maltose-binding protein

2016 ◽  
Vol 62 (3) ◽  
pp. 377-382
Author(s):  
David S Waugh
Keyword(s):  
Escherichia Coli ◽  
Recombinant Proteins ◽  
Inclusion Bodies ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Review Article ◽  
Biologically Active ◽  
Active Protein ◽  
Inactive Form ◽  
Solubility Enhancers

A common problem encountered during the production of recombinant proteins, particularly in bacteria, is their tendency to accumulate in an insoluble and inactive form (i.e., as inclusion bodies). Although sometimes it is possible to convert the aggregated material into native, biologically active protein, this is a time-consuming, costly, and uncertain undertaking. Consequently, a general means of circumventing the formation of inclusion bodies is highly desirable. During the 1990s, it was serendipitously discovered that certain highly soluble proteins have the ability to enhance the solubility of their fusion partners, thereby preventing them from forming insoluble aggregates. In the ensuing years, Escherichia coli maltose-binding protein (MBP) has emerged as one of the most effective solubility enhancers. Moreover, once rendered soluble by fusion to MBP, many proteins are able to fold into their biologically active conformations. This brief review article focuses on our current understanding of what makes MBP such an effective solubility enhancer and how it facilitates the proper folding of its fusion partners.

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