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Unveiling the structure-emulsifying function relationship of truncated recombinant forms of the SA01-OmpA protein opens up a new vista in bioemulsifiers.

Naeema Mohseni SaniMahbubeh TalaeeAli AkbariFaranak AshooriJavad ZamaniAli A KermaniHossein Shahbani ZahiriJohn PresleyHojatollah ValiKambiz Akbari Noghabi
Published in: Microbiology spectrum (2024)
Previous research (Shahryari et al. 2021, mSystems 6: e01175-20) introduced and characterized the SA01-OmpA protein as a multifaceted protein with a variety of functions, including maintaining cellular homeostasis under oxidative stress conditions, biofilm formation, outer membrane vesicles (OMV) biogenesis, and beneficial emulsifying capacity. By truncating the SA01-OmpA protein, the current study presents a unique method for developing protein-type bioemulsifiers. The findings indicate that the N-terminally truncated SA01-OmpA (NT-OmpA) has the potential to fully replace full-length SA01-OmpA as a novel bioemulsifier with significant emulsifying activity. This study opens up a new frontier in bioemulsifiers, shedding light on a possible relationship between the structure and activity of SA01-OmpA truncated forms.
Keyphrases
  • biofilm formation
  • oxidative stress
  • protein protein
  • pseudomonas aeruginosa
  • staphylococcus aureus
  • binding protein
  • escherichia coli
  • dna damage
  • risk assessment
  • cystic fibrosis