Abstract:
:To obtain the soluble production of recombinant NovQ, it has been constructed into the pET28a system. Unfortunately, NovQ was mostly accumulated as inclusion bodies and existed in insoluble fractions of E. coli cell lysate. Four partners, namely His6, TrxA, GST and MBP, were investigated in fusion expression and co-expression to achieve soluble expression in E. coli strains BL21 (DE3) and Rosetta™ (DE3). MBP fusion expression revealed a forceful function in enhancing solubility compared with others, in which the soluble protein was approximately 70% of the total cellular proteins in E. coli. Improvement of rare tRNA abundance promoted the yield of total recombinant protein and the expression level of soluble protein. Besides, one-step purification method was applied and the purity of recombinant protein obtained using Ni-NTA resin was over 90%, where soluble recombinant MBP-NovQ was cleaved using TEV protease in vitro. This method could be an ideal method for soluble expression of ABBA prenyltransferases in E. coli.
journal_name
Bioprocess Biosyst Engjournal_title
Bioprocess and biosystems engineeringauthors
Ni W,Liu H,Wang P,Wang L,Sun X,Wang H,Zhao G,Zheng Zdoi
10.1007/s00449-018-2050-9subject
Has Abstractpub_date
2019-03-01 00:00:00pages
465-474issue
3eissn
1615-7591issn
1615-7605pii
10.1007/s00449-018-2050-9journal_volume
42pub_type
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