Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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A New Protein of ${\alpha}$-Amylase Activity from Lactococcus lactis

  • Wasko, Adam (Department of Biotechnology, Human Nutrition and Food Commodities, University of Life Sciences in Lublin) ;
  • Polak-Berecka, Magdalena (Department of Biotechnology, Human Nutrition and Food Commodities, University of Life Sciences in Lublin) ;
  • Targonski, Zdzislaw (Department of Biotechnology, Human Nutrition and Food Commodities, University of Life Sciences in Lublin)
  • Received : 2010.02.02
  • Accepted : 2010.06.02
  • Published : 2010.09.28
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Abstract

An extracellular ${\alpha}$-amylase from Lactococcus lactis IBB500 was purified and characterized. The optimum conditions for the enzyme activity were a pH of 4.5, temperature of $35^{\circ}C$, and enzyme molecular mass of 121 kDa. The genome analysis and a plasmid curing experiment indicated that $amy^+$ genes were located in a plasmid of 30 kb. An analysis of the phylogenetic relationships strongly supported a hypothesis of horizontal gene transfer. A strong homology was found for the peptides with the sequence of ${\alpha}$-amylases from Ralstonia pikettii and Ralstonia solanacearum. The protein with ${\alpha}$-amylase activity purified in this study is the first one described for the Lactococcus lactis species, and this paper is the first report on a Lactococcus lactis strain belonging to the amylolytic lactic acid bacteria (ALAB).

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References

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