Release of periplasmic enzymes and other physiological effects of β‐lactamase overproduction in Escherichia coli

TLDR: When Escherichia coli containing the plasmid ptac11 is induced with 10−4 M isopropyl‐β‐thiogalactopyranoside (IPTG), 90% of the β‐lactamase activity of an overnight culture is present in the medium and the level of two membrane proteins, OmpA and OmpC, is decreased.

Abstract: When Escherichia coli containing the plasmid ptac11 is induced with 10(-4) M isopropyl-beta-thiogalactopyranoside (IPTG), 90% of the beta-lactamase activity of an overnight culture is present in the medium. The high extracellular activity of beta-lactamase does not result from cell lysis but from an increase in the permeability of the outer membrane. The excreting cells release several other periplasmic enzymes into the extracellular fluid and are more sensitive to lysis by detergents. It was also shown that in these cells the level of two membrane proteins, OmpA and OmpC, is decreased. None of these phenomena were observed with the plasmid pDW17, which has a mutation in the tac promoter that reduces its activity to one fourth of the tac promoter.