SELECTIVE RELEASE OF THE PERIPLASMIC ENZYME BETA-LACTAMASE FROM ESCHERICHIA-COLI WITH TETRADECYL BETAINATE

The periplasmic enzyme beta-lactamase was selectively released from Es cherichia coli K12 by the amphiphilic quaternary ammonium compound tet radecyl betainate at certain concentration intervals. At low concentra tions little enzyme was released, and at high concentrations enzyme in activation occurred. Greater effects of tetradecyl betainate were seen both with respect to release and inactivation at higher pH. At interm ediate concentrations of tetradecyl betainate high yields of beta-lact amase were obtained with no detectable contribution of the cytoplasmic marker beta-galactosidase. The highest yields of beta-lactamase activ ity were obtained when high concentrations of salt were added 1 min af ter permeation of the bacteria with tetradecyl betainate.