High level production of Escherichia coli outer membrane proteins OmpA and OmpF intracellularly in Bacillus subtilis

FEMS Microbiol Lett. 1991 Sep 15;67(1):29-33. doi: 10.1016/0378-1097(91)90438-g.

Abstract

A high yield of Escherichia coli outer membrane proteins OmpA (about 200 mg/l) and OmpF (about 100 mg/l) was obtained in Bacillus subtilis when produced intracellularly. The yield was more than 100-fold higher than the yield of these proteins by a similar vector containing the complete signal sequence of alpha-amylase of B. amyloliquefaciens. Both proteins isolated after breakage of the B. subtilis cells by low-speed centrifugation were about 70% pure and could be solubilized by Sarkosyl, SDS and guanidine hydrochloride.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / genetics*
  • Bacterial Outer Membrane Proteins / biosynthesis
  • Bacterial Outer Membrane Proteins / genetics*
  • Bacterial Outer Membrane Proteins / isolation & purification
  • Cloning, Molecular
  • DNA, Recombinant / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / genetics*
  • Molecular Sequence Data
  • Plasmids
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / isolation & purification

Substances

  • Bacterial Outer Membrane Proteins
  • DNA, Recombinant
  • Recombinant Proteins