Abstract
A novel 54.3 kDa leucine aminopeptidase (LAP) from Lactococcus lactis subsp. lactis cultured in skim milk was purified by using (NH 4) 2SO 4 fractionation, and chromatography on diethylaminoethyl (DEAE)-Toyopearl and hydroxylapatite. The aminopeptidase activity was optimal at pH 7.0 and 35 °C; completely inhibited by EDTA (ethylene diamine tetraacetic acid), chelating agents, sodium iodoacetate, and Ag + ions and strongly inactivated by bestatin and N-ethylmaleimide, but stimulated by Co 2+ ions. It differed in optimum pH and temperature from other reported bacterial aminopeptidases.
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