Open AccessSelective release of the periplasmic enzyme β‐lactamase from Escherichia coli with tetradecyl betainate
Author(s) -
Ahlström Britta,
Edebo Lars
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06859.x
Subject(s) - periplasmic space , enzyme , chemistry , ammonium , bacteria , escherichia coli , biochemistry , enzyme assay , chromatography , biology , organic chemistry , genetics , gene
The periplasmic enzyme β‐lactamase was selectively released from Escherichia coli K12 by the amphiphilic quaternary ammonium compound tetradecyl betainate at certain concentration intervals. At low concentrations little enzyme was released, and at high concentrations enzyme inactivation occurred. Greater effects of tetradecyl betainate were seen both with respect to release and inactivation at higher pH. At intermediate concentrations of tetradecyl betainate high yields of β‐lactamase were obtained with no detectable contribution of the cytoplasmic marker β‐galactosidase. The highest yields of β‐lactmase activity were obtained when high concentrations of salt were added 1 min after permeation of the bacteria with tetradecyl betainate.