Journal of Microbiology and Biotechnology

  • 제20권9호
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  • Pages.1307-1313
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  • 2010
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  • 1017-7825(pISSN)
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  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
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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)
  • 투고 : 2010.02.02
  • 심사 : 2010.06.02
  • 발행 : 2010.09.28
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초록

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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