Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers.

Abstract:

:Escherichia coli maltose-binding protein (MBP) is frequently used as an affinity tag to facilitate the purification of recombinant proteins. An important additional attribute of MBP is its remarkable ability to enhance the solubility of its fusion partners. MBPs are present in a wide variety of microorganisms including both mesophilic and thermophilic bacteria and archaea. In the present study, we compared the ability of MBPs from six diverse microorganisms (E. coli, Pyrococcus furiosus, Thermococcus litoralis, Vibrio cholerae, Thermotoga maritima, and Yersinia pestis) to promote the solubility of eight different aggregation-prone proteins in E. coli. In contrast to glutathione S-transferase (GST), all of these MBPs proved to be effective solubility enhancers and some of them were even more potent solubilizing agents than E. coli MBP.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Fox JD,Routzahn KM,Bucher MH,Waugh DS

doi

10.1016/s0014-5793(03)00070-x

keywords:

subject

Has Abstract

pub_date

2003-02-27 00:00:00

pages

53-7

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S001457930300070X

journal_volume

537

pub_type

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