Cloning, expression and purification of d-tagatose 3-epimerase gene from Escherichia coli JM109.

Abstract:

:An unknown d-tagatose 3-epimerase (DTE) containing a IoIE domain was identified and cloned from Escherichia coli. This gene was subcloned into the prokaryotic expression vector pET-15b, and induced by IPTG in E. coli BL21 expression system. Through His-select gel column purification and fast-protein liquid chromatography, highly purified and stable DTE protein was produced. The molecular weight of the DTE protein was estimated to be 29.8kDa. The latest 83 DTE sequences from public database were selected and analyzed by molecular clustering, multi-sequence alignment. DTEs were roughly divided into five categories.

journal_name

Protein Expr Purif

authors

He X,Zhou X,Yang Z,Xu L,Yu Y,Jia L,Li G

doi

10.1016/j.pep.2015.06.015

subject

Has Abstract

pub_date

2015-10-01 00:00:00

pages

77-81

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(15)30003-6

journal_volume

114

pub_type

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