A simple and rapid protein purification method based on cell-surface display of SUMO-fused recombinant protein and Ulp1 protease.

ABSTRACT: The development of novel methods for highly efficient protein purification remains a research focus in the biotechnology field because conventional purification approaches, including affinity purification, gel filtration, and ion-exchange chromatography, require complex manipulation steps and are costly. Here, we describe a simple and rapid protein purification strategy in which the SUMO tag and Ulp1 protease are surface-displayed separately on Escherichia coli cells. After protein induction, the cells are harvested, resuspended in cleavage buffer, and incubated together for cleavage. In this approach, the surface-displayed Ulp1 cleaves the membrane-anchored SUMO fusion protein, resulting in the release of the target protein from the C-terminal of SUMO into the solution. The bacterial cell

SUBMITTER: Zhou XF 

PROVIDER: S-EPMC7138890 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature