Evaluation of multiple fused partners on enhancing soluble level of prenyltransferase NovQ in Escherichia coli.

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 Eng

authors

Ni W,Liu H,Wang P,Wang L,Sun X,Wang H,Zhao G,Zheng Z

doi

10.1007/s00449-018-2050-9

subject

Has Abstract

pub_date

2019-03-01 00:00:00

pages

465-474

issue

3

eissn

1615-7591

issn

1615-7605

pii

10.1007/s00449-018-2050-9

journal_volume

42

pub_type

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