Soluble Expression and Purification of the SUMO?鄄Heparanase I Fusion Enzyme

doi:10.3969/j.issn.1673-1689.2016.03.015

Home > Archive>Volume 35, Issue 3, 2016 >318-323. DOI:10.3969/j.issn.1673-1689.2016.03.015

Soluble Expression and Purification of the SUMO?鄄Heparanase I Fusion Enzyme
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                        10.3969/j.issn.1673-1689.2016.03.015
                    
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Heparinase I cloned from Flavobacterium heparinum was widely used in the preparation of LMWH（low molecular weight heparin）. However，the formation of inclusion bodies when expressed in Escherichia coli limits its application in a large scale. In this study，the soluble partner，small ubiquitin-like modifier（SUMO），was fused to the N-terminus of Hep I gene with a C-terminal 6×histidine tag. SDS-PAGE analysis of total protein in bacteria and soluble fractions indicated that the portion of the soluble Heparinase I fused with SUMO to the N-terminus was significantly enhanced. After purified by the nickel-chelate chromatography，the resulting fusion enzyme could be used directly without removing the fusion SUMO tag，which made the wide application of Heparinase I feasible.

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ZHAO Shancheng, WANG Zhen, CHENG Yongmei, CHEN Jinghua. Soluble Expression and Purification of the SUMO?鄄Heparanase I Fusion Enzyme[J]. Journal of Food Science and Biotechnology,2016,35(3):318-323.

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Online: November 01,2016
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