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 Purifjournal_title
Protein expression and purificationauthors
He X,Zhou X,Yang Z,Xu L,Yu Y,Jia L,Li Gdoi
10.1016/j.pep.2015.06.015subject
Has Abstractpub_date
2015-10-01 00:00:00pages
77-81eissn
1046-5928issn
1096-0279pii
S1046-5928(15)30003-6journal_volume
114pub_type
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