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- W2079671566 abstract "A novel 54.3 kDa leucine aminopeptidase (LAP) from Lactococcus lactis subsp. lactis cultured in skim milk was purified by using (NH4)2SO4 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 Co2+ ions. It differed in optimum pH and temperature from other reported bacterial aminopeptidases." @default.
- W2079671566 created "2016-06-24" @default.
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- W2079671566 date "2011-07-01" @default.
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- W2079671566 title "Purification and characterisation of a leucine aminopeptidase from Lactococcus lactis subsp. lactis cultured in skim milk" @default.
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- W2079671566 doi "https://doi.org/10.1016/j.idairyj.2011.02.007" @default.
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