Work

Cloning and heterologous expression of recombinant microcin S in Escherichia coli.

Year: 2026

Type: article

Abstract: BL21 Star™ (DE3). Furthermore, the expressed protein exhibited 60% solubility, which could be partially attributed to its fusion with MBP. In the current study, the production of recombinant MccS was reported for the first time. The designed expression system proved to be efficient in producing the desired protein. Therefore, in future studies, it will be important to investigate the antibacterial and probiotic activity of MccS. Additionally, it may also act as an efficient biological preservative.

Source: PubMed Central

DOI: 10.22099/mbrc.2026.56252.2306

Authors: Vahid Dianatpur, Seyed Shahram Shekarforoush, Abdollah Derakhshandeh, Azar Motamedi-Boroojeni, Vida Eraghi, Farhid Hemmatzadeh

Institutions: Shiraz University, University of Zagreb, Adelaide University, The University of Adelaide

Language: English

Topic: Antimicrobial Peptides and Activities

Subfield: Microbiology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: green

Funder: Shiraz University

OpenAlex ID: W7225258403