Purification and Characterization of Invertase from Lactobacillus reuteri CRL 1100 |
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Authors: | Silvia Cuezzo de Ginés María C Maldonado Graciela Font de Valdez |
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Institution: | (1) Cátedra de Bioquímica Clínica III, Universidad Nacional de Tucumán, Argentina , AR;(2) Cátedra de Microbiología Industrial, Universidad Nacional de Tucumán, Argentina , AR;(3) Cátedra de Microbiología Superior, Universidad Nacional de Tucumán, Argentina , AR;(4) Centro de Referencia para Lactobacilos (CERELA), Chacabuco 145, 4000 S.M. de Tucumán, Argentina , AR |
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Abstract: | The invertase of Lactobacillus reuteri CRL 1100 is a glycoprotein composed by a single subunit with a molecular weight of 58 kDa. The enzyme was stable below 45°C
over a wide pH range (4.5–7.0) with maximum activity at pH 6.0 and 37°C. The invertase activity was significantly inhibited
by bivalent metal ions (Ca++, Cu++, Cd++, and Hg++), β-mercaptoethanol, and dithiothreitol and partially improved by ethylenediaminetetraacetic acid. The enzyme was purified
32 times over the crude extract by gel filtration and ion-exchange chromatography with a recovery of 17%. The K
m
and Vmax values for sucrose were 6.66 mM and 0.028 μmol/min, respectively. An invertase is purified and characterized for the first
time in Lactobacillus, and it proved to be a β-fructofuranosidase.
Received: 13 August 1999 / Accepted: 15 September 1999 |
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