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- W2006667555 abstract "The factors involved in the pathogenesis of Bacillus cereus (B. cereus) in non-gastrointestinal diseases are poorly investigated. Some researchers suggest that B. cereus proteases may be involved in these illnesses. The aim of this work was to purify and characterize a protease isolated from a virulent strain of B. cereus to explain its assumptive damaging effect. The enzyme was purified in a four-step procedure involving ammonium sulfate fractionation, acetone precipitation, Bio-Gel filtration and column chromatography on DEAE-cellulose (DE-52 cellulose). The enzyme appeared homogenous using disc electrophoresis. The specific activity of the protease was 72 U/mg of protein. The enzyme was shown to have a relative molecular mass of 29 kDa. The protease was most active at pH 7.0 and 40 degrees C with haemoglobin as the substrate. The enzyme was made completely inactive by ethylenediaminetetraacetic acid (EDTA), beta-mercaptoethanol, dithiothreitol (DTT) and benzamidine (at a concentration of 1 mM) and by diisopropylfluorophosphate (DIPF), L-cysteine, L-histidine, 1,10-phenanthroline (at a concentration of 10 mM). Divalent cations, especially Ca2+ increased enzyme activity. The enzyme hydrolysed haemoglobin, albumin and casein as the substrates. With haemoglobin and albumin as the substrates Michaelis-Menten kinetics was observed. The obtained Km values were 86 +/- 40 microM (SD, n = 3) and 340 +/- 100 microM (SD, n = 3) for haemoglobin and albumin, respectively. The corresponding Vmax values were 1.26 +/- 0.1 (SD, n = 3) and 0.38 +/- 0.07 (SD, n = 3) mumol of tyrosine liberated per min, per ml, and per mg, while those for casein were not determined. It is concluded that this enzyme is a metal-chelator-sensitive, neutral protease damaging haemoglobin and albumin." @default.
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- W2006667555 date "1998-05-01" @default.
- W2006667555 modified "2023-10-16" @default.
- W2006667555 title "Purification and partial characterization of a neutral protease from a virulent strain of Bacillus cereus" @default.
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- W2006667555 doi "https://doi.org/10.1016/s1357-2725(98)00007-7" @default.
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