|Table of Contents|

Low Concentration of Salt Triggers Elastin-like Polypeptides Inverse Transition to Purify 1,3-propanediol Oxidoreductase(PDF)

Chinese Journal of Applied & Environmental Biology[ISSN:1006-687X/CN:51-1482/Q]

Issue:
2013 04
Page:
709-712
Research Field:
Articles
Publishing date:

Info

Title:
Low Concentration of Salt Triggers Elastin-like Polypeptides Inverse Transition to Purify 1,3-propanediol Oxidoreductase
Author(s):
GE Huihua HUANG Zhihong WANG Wenyan ZHANG Shiran ZHANG Guangya
(Department of Bioengineering and Biotechnology, Huaqiao University, Xiamen 361021, China)
Keywords:
elastin-like polypeptides purification tag inverse temperature transition recombinant enzyme purification non-chromatographic
CLC:
Q814
PACS:
DOI:
10.3724/SP.J.1145.2013.00709
DocumentCode:

Abstract:
Elastin-like polypeptides have been widely used as the purification tag. Non-chromatographic purification of ELPs fusion proteins, termed inverse transition cycling (ITC), exploits the reversible soluble-insoluble phase transition behavior imparted by the ELPs tag. This study found that the novel ELPs tag could purify 1,3-propanediol oxidoreductase (PDOR) efficiently. The ELPs aggregated with 0.8 mol/L Na2CO3 at room temperature, and then PDOR, which was linked with the ELPs, was purified by ITC. The purity could reach about 98%, and the purification fold was above 8, about 7 times that of His-tag purification method. By comparing the properties of the purified fusion ELPs-PDOR and His-PDOR, we found that ELPs tag hardly affects the target protein, suggesting that it can be used during the biocatalysis process. The method with low salt concentration to induce the phase transition of ELPs can avoid potential adverse effect on enzyme structure and property, thus being advantageous in protein purification. Fig 3, Tab 2, Ref 17

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Last Update: 2013-08-22