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.
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Received: 13 August 1999 / Accepted: 15 September 1999
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Cuezzo de Ginés, S., Maldonado, M. & Font de Valdez, G. Purification and Characterization of Invertase from Lactobacillus reuteri CRL 1100. Curr Microbiol 40, 181–184 (2000). https://doi.org/10.1007/s002849910036
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DOI: https://doi.org/10.1007/s002849910036